Potassium in PDB 3q9f: Crystal Structure of Apah Complexed with Caps
Protein crystallography data
The structure of Crystal Structure of Apah Complexed with Caps, PDB code: 3q9f
was solved by
P.M.Lombardi,
D.W.Christianson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.35
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
118.252,
119.651,
119.571,
98.34,
94.94,
114.95
|
R / Rfree (%)
|
18.9 /
22.5
|
Other elements in 3q9f:
The structure of Crystal Structure of Apah Complexed with Caps also contains other interesting chemical elements:
Potassium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Binding sites:
The binding sites of Potassium atom in the Crystal Structure of Apah Complexed with Caps
(pdb code 3q9f). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 20 binding sites of Potassium where determined in the
Crystal Structure of Apah Complexed with Caps, PDB code: 3q9f:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Potassium binding site 1 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 1 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K342
b:29.6
occ:1.00
|
O
|
A:ASP195
|
2.5
|
26.3
|
1.0
|
OD1
|
A:ASP193
|
2.6
|
30.2
|
1.0
|
O
|
A:LEU217
|
2.6
|
28.8
|
1.0
|
O
|
A:HIS197
|
2.7
|
26.0
|
1.0
|
O
|
A:ASP193
|
2.8
|
28.4
|
1.0
|
OG
|
A:SER216
|
2.9
|
23.9
|
1.0
|
CG
|
A:ASP193
|
3.2
|
29.1
|
1.0
|
C
|
A:ASP193
|
3.5
|
27.5
|
1.0
|
C
|
A:LEU217
|
3.6
|
28.0
|
1.0
|
C
|
A:ASP195
|
3.6
|
26.9
|
1.0
|
C
|
A:HIS197
|
3.6
|
26.1
|
1.0
|
CB
|
A:ASP193
|
3.7
|
27.4
|
1.0
|
N
|
A:ASP195
|
3.7
|
28.7
|
1.0
|
CB
|
A:HIS218
|
3.7
|
21.0
|
1.0
|
N
|
A:LEU217
|
3.9
|
26.8
|
1.0
|
OD2
|
A:ASP193
|
4.0
|
30.0
|
1.0
|
ND1
|
A:HIS218
|
4.1
|
21.4
|
1.0
|
CA
|
A:HIS198
|
4.1
|
25.3
|
1.0
|
C
|
A:VAL194
|
4.1
|
28.8
|
1.0
|
CA
|
A:ASP195
|
4.1
|
27.1
|
1.0
|
CB
|
A:SER216
|
4.2
|
26.0
|
1.0
|
N
|
A:VAL194
|
4.2
|
26.4
|
1.0
|
CB
|
A:ASP195
|
4.2
|
26.9
|
1.0
|
CA
|
A:ASP193
|
4.2
|
28.1
|
1.0
|
N
|
A:HIS198
|
4.3
|
25.3
|
1.0
|
CA
|
A:HIS218
|
4.3
|
25.5
|
1.0
|
N
|
A:HIS218
|
4.3
|
25.5
|
1.0
|
CA
|
A:VAL194
|
4.4
|
27.8
|
1.0
|
N
|
A:GLY199
|
4.4
|
26.1
|
1.0
|
CG
|
A:HIS218
|
4.4
|
20.8
|
1.0
|
CA
|
A:LEU217
|
4.4
|
26.2
|
1.0
|
C
|
A:SER216
|
4.5
|
28.1
|
1.0
|
CA
|
A:SER216
|
4.5
|
27.7
|
1.0
|
C
|
A:HIS198
|
4.5
|
26.9
|
1.0
|
N
|
A:HIS197
|
4.5
|
23.8
|
1.0
|
C
|
A:PHE196
|
4.6
|
27.5
|
1.0
|
O
|
A:HOH374
|
4.6
|
32.2
|
1.0
|
CA
|
A:HIS197
|
4.7
|
25.1
|
1.0
|
O
|
A:VAL194
|
4.7
|
30.5
|
1.0
|
O
|
A:PHE196
|
4.7
|
28.8
|
1.0
|
N
|
A:PHE196
|
4.7
|
26.8
|
1.0
|
|
Potassium binding site 2 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 2 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K344
b:73.8
occ:1.00
|
O
|
A:HOH745
|
2.7
|
37.2
|
1.0
|
OG
|
A:SER292
|
2.7
|
43.0
|
1.0
|
O
|
A:ASP289
|
2.8
|
47.7
|
1.0
|
O
|
A:SER292
|
2.8
|
39.8
|
1.0
|
O
|
A:PHE286
|
2.9
|
33.7
|
1.0
|
O
|
A:GLU287
|
3.1
|
40.2
|
1.0
|
C
|
A:SER292
|
3.4
|
40.5
|
1.0
|
O
|
A:PHE294
|
3.4
|
42.6
|
1.0
|
C
|
A:GLU287
|
3.5
|
41.6
|
1.0
|
CA
|
A:GLU287
|
3.6
|
41.4
|
1.0
|
C
|
A:PHE286
|
3.8
|
35.5
|
1.0
|
CB
|
A:SER292
|
3.9
|
43.1
|
1.0
|
C
|
A:ASP289
|
3.9
|
46.1
|
1.0
|
N
|
A:ASP289
|
4.0
|
46.5
|
1.0
|
CA
|
A:SER292
|
4.0
|
41.7
|
1.0
|
N
|
A:PHE293
|
4.1
|
38.2
|
1.0
|
N
|
A:GLU287
|
4.2
|
38.5
|
1.0
|
N
|
A:SER292
|
4.2
|
43.2
|
1.0
|
N
|
A:PHE294
|
4.2
|
38.6
|
1.0
|
CA
|
A:ASP289
|
4.3
|
46.1
|
1.0
|
CA
|
A:PHE293
|
4.4
|
37.0
|
1.0
|
CB
|
A:ASP289
|
4.4
|
45.5
|
1.0
|
N
|
A:GLN288
|
4.4
|
43.5
|
1.0
|
C
|
A:PHE294
|
4.5
|
40.6
|
1.0
|
C
|
A:PHE293
|
4.7
|
37.3
|
1.0
|
C
|
A:GLN288
|
4.7
|
46.7
|
1.0
|
O
|
A:THR285
|
4.8
|
32.8
|
1.0
|
CB
|
A:GLU287
|
4.9
|
45.8
|
1.0
|
O
|
A:ASP284
|
4.9
|
32.1
|
1.0
|
|
Potassium binding site 3 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 3 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K342
b:32.2
occ:1.00
|
O
|
B:ASP195
|
2.5
|
28.5
|
1.0
|
O
|
B:LEU217
|
2.6
|
29.3
|
1.0
|
OD1
|
B:ASP193
|
2.7
|
31.3
|
1.0
|
OG
|
B:SER216
|
2.7
|
25.3
|
1.0
|
O
|
B:ASP193
|
2.9
|
31.6
|
1.0
|
O
|
B:HIS197
|
2.9
|
28.4
|
1.0
|
CG
|
B:ASP193
|
3.2
|
29.6
|
1.0
|
C
|
B:ASP193
|
3.5
|
30.6
|
1.0
|
CB
|
B:ASP193
|
3.6
|
30.0
|
1.0
|
C
|
B:LEU217
|
3.6
|
28.4
|
1.0
|
C
|
B:ASP195
|
3.6
|
30.9
|
1.0
|
N
|
B:LEU217
|
3.7
|
27.3
|
1.0
|
C
|
B:HIS197
|
3.8
|
29.6
|
1.0
|
N
|
B:ASP195
|
3.8
|
32.4
|
1.0
|
CB
|
B:HIS218
|
3.9
|
26.3
|
1.0
|
CB
|
B:SER216
|
4.0
|
24.3
|
1.0
|
OD2
|
B:ASP193
|
4.0
|
29.5
|
1.0
|
C
|
B:VAL194
|
4.1
|
33.0
|
1.0
|
CA
|
B:ASP193
|
4.2
|
30.6
|
1.0
|
CA
|
B:HIS198
|
4.2
|
28.0
|
1.0
|
CA
|
B:ASP195
|
4.2
|
31.7
|
1.0
|
N
|
B:VAL194
|
4.2
|
31.1
|
1.0
|
ND1
|
B:HIS218
|
4.3
|
25.1
|
1.0
|
CA
|
B:SER216
|
4.3
|
27.1
|
1.0
|
N
|
B:GLY199
|
4.3
|
28.4
|
1.0
|
N
|
B:HIS198
|
4.3
|
28.0
|
1.0
|
C
|
B:SER216
|
4.4
|
26.9
|
1.0
|
CA
|
B:LEU217
|
4.4
|
28.0
|
1.0
|
CB
|
B:ASP195
|
4.4
|
32.5
|
1.0
|
CA
|
B:VAL194
|
4.5
|
31.6
|
1.0
|
N
|
B:HIS218
|
4.5
|
27.1
|
1.0
|
CG
|
B:HIS218
|
4.5
|
24.7
|
1.0
|
CA
|
B:HIS218
|
4.5
|
28.7
|
1.0
|
C
|
B:PHE196
|
4.5
|
30.4
|
1.0
|
C
|
B:HIS198
|
4.6
|
29.0
|
1.0
|
O
|
B:HOH392
|
4.6
|
29.0
|
1.0
|
O
|
B:PHE196
|
4.6
|
31.2
|
1.0
|
N
|
B:HIS197
|
4.6
|
29.5
|
1.0
|
O
|
B:VAL194
|
4.7
|
34.5
|
1.0
|
N
|
B:PHE196
|
4.7
|
29.4
|
1.0
|
CA
|
B:HIS197
|
4.8
|
28.4
|
1.0
|
|
Potassium binding site 4 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 4 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K342
b:29.7
occ:1.00
|
OD1
|
C:ASP193
|
2.4
|
28.5
|
1.0
|
O
|
C:ASP195
|
2.5
|
27.6
|
1.0
|
O
|
C:LEU217
|
2.7
|
27.6
|
1.0
|
OG
|
C:SER216
|
2.8
|
22.6
|
1.0
|
O
|
C:ASP193
|
2.9
|
27.3
|
1.0
|
O
|
C:HIS197
|
2.9
|
26.0
|
1.0
|
CG
|
C:ASP193
|
3.1
|
27.6
|
1.0
|
C
|
C:ASP193
|
3.4
|
25.6
|
1.0
|
CB
|
C:ASP193
|
3.5
|
25.9
|
1.0
|
C
|
C:ASP195
|
3.5
|
27.0
|
1.0
|
N
|
C:ASP195
|
3.6
|
28.8
|
1.0
|
C
|
C:HIS197
|
3.7
|
25.7
|
1.0
|
C
|
C:LEU217
|
3.7
|
26.1
|
1.0
|
N
|
C:LEU217
|
3.9
|
24.5
|
1.0
|
OD2
|
C:ASP193
|
3.9
|
29.2
|
1.0
|
CB
|
C:HIS218
|
3.9
|
21.7
|
1.0
|
CA
|
C:ASP195
|
4.0
|
27.0
|
1.0
|
CB
|
C:ASP195
|
4.0
|
28.2
|
1.0
|
CB
|
C:SER216
|
4.0
|
24.2
|
1.0
|
C
|
C:VAL194
|
4.1
|
28.2
|
1.0
|
N
|
C:VAL194
|
4.1
|
25.6
|
1.0
|
CA
|
C:HIS198
|
4.1
|
25.2
|
1.0
|
CA
|
C:ASP193
|
4.1
|
26.0
|
1.0
|
N
|
C:GLY199
|
4.2
|
25.0
|
1.0
|
N
|
C:HIS198
|
4.2
|
25.0
|
1.0
|
ND1
|
C:HIS218
|
4.3
|
19.7
|
1.0
|
CA
|
C:VAL194
|
4.3
|
25.8
|
1.0
|
CA
|
C:SER216
|
4.4
|
25.9
|
1.0
|
C
|
C:HIS198
|
4.4
|
25.5
|
1.0
|
C
|
C:SER216
|
4.5
|
26.3
|
1.0
|
N
|
C:HIS197
|
4.5
|
24.7
|
1.0
|
CA
|
C:HIS218
|
4.5
|
26.2
|
1.0
|
CA
|
C:LEU217
|
4.5
|
25.2
|
1.0
|
N
|
C:HIS218
|
4.5
|
25.4
|
1.0
|
CG
|
C:HIS218
|
4.6
|
20.4
|
1.0
|
C
|
C:PHE196
|
4.6
|
26.7
|
1.0
|
N
|
C:PHE196
|
4.7
|
25.1
|
1.0
|
CA
|
C:HIS197
|
4.7
|
25.3
|
1.0
|
O
|
C:VAL194
|
4.8
|
30.0
|
1.0
|
O
|
C:HOH444
|
4.8
|
24.5
|
1.0
|
OD1
|
C:ASP195
|
4.9
|
27.7
|
1.0
|
O
|
C:PHE196
|
4.9
|
27.0
|
1.0
|
CG
|
C:ASP195
|
5.0
|
29.1
|
1.0
|
|
Potassium binding site 5 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 5 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K344
b:77.2
occ:1.00
|
OG
|
C:SER292
|
2.6
|
42.1
|
1.0
|
O
|
C:ASP289
|
2.8
|
44.1
|
1.0
|
O
|
C:HOH1274
|
2.8
|
38.8
|
1.0
|
O
|
C:SER292
|
2.8
|
40.6
|
1.0
|
O
|
C:PHE286
|
2.9
|
33.7
|
1.0
|
O
|
C:GLU287
|
3.0
|
41.8
|
1.0
|
C
|
C:GLU287
|
3.4
|
41.4
|
1.0
|
C
|
C:SER292
|
3.4
|
40.6
|
1.0
|
CA
|
C:GLU287
|
3.5
|
41.2
|
1.0
|
O
|
C:PHE294
|
3.5
|
41.1
|
1.0
|
C
|
C:PHE286
|
3.8
|
34.9
|
1.0
|
CB
|
C:SER292
|
3.8
|
42.6
|
1.0
|
N
|
C:ASP289
|
3.8
|
43.8
|
1.0
|
C
|
C:ASP289
|
3.8
|
43.6
|
1.0
|
CA
|
C:SER292
|
4.0
|
41.5
|
1.0
|
N
|
C:PHE293
|
4.1
|
37.8
|
1.0
|
N
|
C:GLU287
|
4.1
|
37.6
|
1.0
|
N
|
C:SER292
|
4.2
|
43.6
|
1.0
|
N
|
C:PHE294
|
4.2
|
37.7
|
1.0
|
CA
|
C:ASP289
|
4.2
|
43.3
|
1.0
|
CB
|
C:ASP289
|
4.2
|
44.7
|
1.0
|
N
|
C:GLN288
|
4.3
|
41.8
|
1.0
|
CA
|
C:PHE293
|
4.4
|
36.8
|
1.0
|
C
|
C:PHE294
|
4.6
|
39.9
|
1.0
|
O
|
C:THR285
|
4.7
|
32.9
|
1.0
|
C
|
C:PHE293
|
4.7
|
37.2
|
1.0
|
C
|
C:GLN288
|
4.7
|
44.1
|
1.0
|
CB
|
C:GLU287
|
4.8
|
44.8
|
1.0
|
O
|
C:ASP284
|
4.8
|
32.0
|
1.0
|
CA
|
C:GLN288
|
4.9
|
44.6
|
1.0
|
C
|
C:THR285
|
5.0
|
31.9
|
1.0
|
|
Potassium binding site 6 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 6 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K342
b:29.5
occ:1.00
|
OD1
|
D:ASP193
|
2.5
|
26.1
|
1.0
|
O
|
D:ASP195
|
2.6
|
23.0
|
1.0
|
O
|
D:LEU217
|
2.7
|
29.3
|
1.0
|
OG
|
D:SER216
|
2.8
|
23.6
|
1.0
|
O
|
D:ASP193
|
2.8
|
24.4
|
1.0
|
O
|
D:HIS197
|
2.9
|
26.2
|
1.0
|
CG
|
D:ASP193
|
3.1
|
26.2
|
1.0
|
C
|
D:ASP193
|
3.5
|
25.1
|
1.0
|
CB
|
D:ASP193
|
3.6
|
25.4
|
1.0
|
C
|
D:ASP195
|
3.6
|
24.4
|
1.0
|
C
|
D:LEU217
|
3.7
|
27.8
|
1.0
|
C
|
D:HIS197
|
3.7
|
28.1
|
1.0
|
N
|
D:ASP195
|
3.8
|
24.6
|
1.0
|
CB
|
D:HIS218
|
3.8
|
22.7
|
1.0
|
N
|
D:LEU217
|
3.9
|
25.6
|
1.0
|
OD2
|
D:ASP193
|
3.9
|
28.6
|
1.0
|
CB
|
D:SER216
|
4.0
|
22.7
|
1.0
|
C
|
D:VAL194
|
4.1
|
26.9
|
1.0
|
CA
|
D:HIS198
|
4.1
|
29.0
|
1.0
|
CA
|
D:ASP195
|
4.2
|
24.6
|
1.0
|
N
|
D:VAL194
|
4.2
|
26.0
|
1.0
|
CA
|
D:ASP193
|
4.2
|
25.4
|
1.0
|
N
|
D:GLY199
|
4.3
|
30.5
|
1.0
|
N
|
D:HIS198
|
4.3
|
28.4
|
1.0
|
ND1
|
D:HIS218
|
4.3
|
20.2
|
1.0
|
CB
|
D:ASP195
|
4.3
|
26.6
|
1.0
|
CA
|
D:SER216
|
4.4
|
24.7
|
1.0
|
CA
|
D:VAL194
|
4.4
|
26.4
|
1.0
|
C
|
D:SER216
|
4.4
|
25.4
|
1.0
|
CA
|
D:HIS218
|
4.5
|
25.4
|
1.0
|
C
|
D:HIS198
|
4.5
|
29.8
|
1.0
|
CA
|
D:LEU217
|
4.5
|
25.7
|
1.0
|
CG
|
D:HIS218
|
4.5
|
21.5
|
1.0
|
N
|
D:HIS218
|
4.5
|
26.4
|
1.0
|
N
|
D:HIS197
|
4.5
|
27.5
|
1.0
|
C
|
D:PHE196
|
4.6
|
27.1
|
1.0
|
O
|
D:VAL194
|
4.7
|
26.5
|
1.0
|
O
|
D:HOH596
|
4.7
|
23.5
|
1.0
|
N
|
D:PHE196
|
4.7
|
26.3
|
1.0
|
O
|
D:PHE196
|
4.8
|
27.1
|
1.0
|
CA
|
D:HIS197
|
4.8
|
27.0
|
1.0
|
OD1
|
D:ASP195
|
4.9
|
26.6
|
1.0
|
|
Potassium binding site 7 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 7 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K344
b:69.9
occ:1.00
|
OG
|
D:SER292
|
2.6
|
44.0
|
1.0
|
O
|
D:HOH1275
|
2.7
|
59.9
|
1.0
|
O
|
D:ASP289
|
2.8
|
44.8
|
1.0
|
O
|
D:SER292
|
2.8
|
39.6
|
1.0
|
O
|
D:PHE286
|
3.0
|
33.6
|
1.0
|
O
|
D:HOH1273
|
3.3
|
42.3
|
1.0
|
C
|
D:SER292
|
3.3
|
41.5
|
1.0
|
O
|
D:GLU287
|
3.3
|
38.8
|
1.0
|
O
|
D:PHE294
|
3.5
|
45.1
|
1.0
|
C
|
D:GLU287
|
3.6
|
40.1
|
1.0
|
CA
|
D:GLU287
|
3.6
|
40.1
|
1.0
|
CB
|
D:SER292
|
3.7
|
43.9
|
1.0
|
CA
|
D:SER292
|
3.9
|
43.1
|
1.0
|
C
|
D:ASP289
|
3.9
|
43.3
|
1.0
|
N
|
D:PHE293
|
3.9
|
40.0
|
1.0
|
C
|
D:PHE286
|
4.0
|
34.5
|
1.0
|
N
|
D:PHE294
|
4.0
|
41.2
|
1.0
|
N
|
D:SER292
|
4.1
|
44.2
|
1.0
|
N
|
D:ASP289
|
4.2
|
43.2
|
1.0
|
CA
|
D:PHE293
|
4.2
|
40.4
|
1.0
|
N
|
D:GLU287
|
4.2
|
37.2
|
1.0
|
N
|
D:GLN288
|
4.4
|
41.4
|
1.0
|
CA
|
D:ASP289
|
4.5
|
44.2
|
1.0
|
C
|
D:PHE293
|
4.5
|
40.3
|
1.0
|
CB
|
D:ASP289
|
4.5
|
45.5
|
1.0
|
C
|
D:PHE294
|
4.5
|
43.9
|
1.0
|
C
|
D:GLN288
|
4.8
|
44.5
|
1.0
|
CB
|
D:GLU287
|
4.8
|
42.8
|
1.0
|
O
|
D:THR285
|
4.8
|
31.6
|
1.0
|
CA
|
D:PHE294
|
4.9
|
41.9
|
1.0
|
O
|
D:ASP284
|
5.0
|
35.6
|
1.0
|
|
Potassium binding site 8 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 8 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K342
b:33.8
occ:1.00
|
O
|
E:LEU217
|
2.6
|
30.6
|
1.0
|
O
|
E:ASP195
|
2.6
|
27.3
|
1.0
|
OD1
|
E:ASP193
|
2.7
|
31.1
|
1.0
|
O
|
E:HIS197
|
2.7
|
27.9
|
1.0
|
OG
|
E:SER216
|
2.9
|
21.8
|
1.0
|
O
|
E:ASP193
|
3.0
|
29.3
|
1.0
|
CG
|
E:ASP193
|
3.3
|
32.0
|
1.0
|
C
|
E:ASP193
|
3.6
|
29.9
|
1.0
|
C
|
E:ASP195
|
3.6
|
28.7
|
1.0
|
C
|
E:HIS197
|
3.6
|
27.7
|
1.0
|
C
|
E:LEU217
|
3.7
|
29.7
|
1.0
|
N
|
E:ASP195
|
3.7
|
28.6
|
1.0
|
CB
|
E:ASP193
|
3.7
|
30.3
|
1.0
|
CB
|
E:HIS218
|
3.8
|
26.1
|
1.0
|
N
|
E:LEU217
|
3.9
|
28.9
|
1.0
|
CA
|
E:ASP195
|
4.0
|
28.9
|
1.0
|
CA
|
E:HIS198
|
4.0
|
28.0
|
1.0
|
CB
|
E:ASP195
|
4.1
|
30.4
|
1.0
|
C
|
E:VAL194
|
4.1
|
29.6
|
1.0
|
OD2
|
E:ASP193
|
4.1
|
31.2
|
1.0
|
N
|
E:HIS198
|
4.1
|
26.3
|
1.0
|
CB
|
E:SER216
|
4.2
|
26.2
|
1.0
|
N
|
E:VAL194
|
4.2
|
30.2
|
1.0
|
CA
|
E:ASP193
|
4.3
|
30.4
|
1.0
|
ND1
|
E:HIS218
|
4.3
|
26.7
|
1.0
|
N
|
E:GLY199
|
4.3
|
29.2
|
1.0
|
O
|
E:HOH361
|
4.4
|
22.6
|
1.0
|
N
|
E:HIS197
|
4.4
|
28.2
|
1.0
|
CA
|
E:VAL194
|
4.4
|
30.0
|
1.0
|
C
|
E:HIS198
|
4.5
|
28.3
|
1.0
|
CA
|
E:HIS218
|
4.5
|
28.7
|
1.0
|
CA
|
E:LEU217
|
4.5
|
28.9
|
1.0
|
C
|
E:PHE196
|
4.5
|
30.7
|
1.0
|
CG
|
E:HIS218
|
4.5
|
29.1
|
1.0
|
N
|
E:HIS218
|
4.5
|
27.1
|
1.0
|
CA
|
E:SER216
|
4.5
|
27.8
|
1.0
|
C
|
E:SER216
|
4.5
|
28.8
|
1.0
|
CA
|
E:HIS197
|
4.6
|
27.4
|
1.0
|
N
|
E:PHE196
|
4.7
|
30.3
|
1.0
|
O
|
E:VAL194
|
4.7
|
31.7
|
1.0
|
O
|
E:PHE196
|
4.7
|
29.6
|
1.0
|
ND1
|
E:HIS158
|
5.0
|
28.5
|
1.0
|
|
Potassium binding site 9 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 9 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 9 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K344
b:96.5
occ:1.00
|
O
|
E:SER292
|
2.6
|
51.0
|
1.0
|
O
|
E:HOH1288
|
2.7
|
37.2
|
1.0
|
O
|
E:HOH1289
|
2.8
|
76.2
|
1.0
|
O
|
E:PHE286
|
3.1
|
42.1
|
1.0
|
O
|
E:GLU287
|
3.2
|
48.4
|
1.0
|
O
|
E:ASP289
|
3.3
|
53.7
|
1.0
|
C
|
E:SER292
|
3.3
|
50.3
|
1.0
|
O
|
E:PHE294
|
3.4
|
45.3
|
1.0
|
C
|
E:GLU287
|
3.5
|
49.1
|
1.0
|
N
|
E:ASP289
|
3.6
|
53.5
|
1.0
|
CA
|
E:GLU287
|
3.9
|
48.0
|
1.0
|
N
|
E:PHE293
|
4.0
|
48.1
|
1.0
|
N
|
E:PHE294
|
4.0
|
46.1
|
1.0
|
CB
|
E:ASP289
|
4.0
|
54.5
|
1.0
|
CA
|
E:PHE293
|
4.0
|
45.1
|
1.0
|
C
|
E:ASP289
|
4.1
|
54.1
|
1.0
|
C
|
E:PHE286
|
4.1
|
42.5
|
1.0
|
CA
|
E:ASP289
|
4.1
|
53.4
|
1.0
|
N
|
E:GLN288
|
4.2
|
50.6
|
1.0
|
CA
|
E:SER292
|
4.2
|
51.6
|
1.0
|
CB
|
E:SER292
|
4.2
|
53.1
|
1.0
|
C
|
E:PHE293
|
4.4
|
45.4
|
1.0
|
N
|
E:GLU287
|
4.4
|
43.9
|
1.0
|
N
|
E:SER292
|
4.5
|
54.0
|
1.0
|
C
|
E:PHE294
|
4.5
|
45.4
|
1.0
|
C
|
E:GLN288
|
4.5
|
52.9
|
1.0
|
CA
|
E:GLN288
|
4.7
|
52.9
|
1.0
|
O
|
E:ASP284
|
4.8
|
38.9
|
1.0
|
CA
|
E:PHE294
|
4.9
|
45.0
|
1.0
|
|
Potassium binding site 10 out
of 20 in 3q9f
Go back to
Potassium Binding Sites List in 3q9f
Potassium binding site 10 out
of 20 in the Crystal Structure of Apah Complexed with Caps
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 10 of Crystal Structure of Apah Complexed with Caps within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K342
b:31.0
occ:1.00
|
OD1
|
F:ASP193
|
2.5
|
34.2
|
1.0
|
O
|
F:HIS197
|
2.6
|
33.1
|
1.0
|
O
|
F:LEU217
|
2.6
|
37.0
|
1.0
|
O
|
F:ASP195
|
2.7
|
30.1
|
1.0
|
O
|
F:ASP193
|
2.7
|
32.4
|
1.0
|
OG
|
F:SER216
|
2.8
|
35.6
|
1.0
|
CG
|
F:ASP193
|
3.2
|
35.3
|
1.0
|
C
|
F:ASP193
|
3.4
|
32.5
|
1.0
|
C
|
F:LEU217
|
3.6
|
35.7
|
1.0
|
CB
|
F:ASP193
|
3.6
|
33.4
|
1.0
|
C
|
F:HIS197
|
3.6
|
32.6
|
1.0
|
C
|
F:ASP195
|
3.7
|
30.9
|
1.0
|
N
|
F:ASP195
|
3.7
|
32.6
|
1.0
|
N
|
F:LEU217
|
3.8
|
33.6
|
1.0
|
CB
|
F:HIS218
|
3.8
|
33.6
|
1.0
|
CB
|
F:SER216
|
4.0
|
34.3
|
1.0
|
C
|
F:VAL194
|
4.1
|
33.7
|
1.0
|
OD2
|
F:ASP193
|
4.1
|
36.4
|
1.0
|
CA
|
F:HIS198
|
4.1
|
32.8
|
1.0
|
ND1
|
F:HIS218
|
4.1
|
34.8
|
1.0
|
CA
|
F:ASP195
|
4.1
|
31.3
|
1.0
|
N
|
F:VAL194
|
4.2
|
32.4
|
1.0
|
CA
|
F:ASP193
|
4.2
|
32.6
|
1.0
|
CB
|
F:ASP195
|
4.2
|
31.3
|
1.0
|
N
|
F:HIS198
|
4.3
|
32.0
|
1.0
|
N
|
F:GLY199
|
4.3
|
31.9
|
1.0
|
CA
|
F:VAL194
|
4.3
|
34.0
|
1.0
|
CA
|
F:SER216
|
4.4
|
33.8
|
1.0
|
C
|
F:SER216
|
4.4
|
32.9
|
1.0
|
CG
|
F:HIS218
|
4.4
|
34.5
|
1.0
|
CA
|
F:LEU217
|
4.5
|
35.2
|
1.0
|
N
|
F:HIS218
|
4.5
|
35.3
|
1.0
|
CA
|
F:HIS218
|
4.5
|
34.5
|
1.0
|
C
|
F:HIS198
|
4.5
|
32.3
|
1.0
|
C
|
F:PHE196
|
4.6
|
33.2
|
1.0
|
N
|
F:HIS197
|
4.6
|
33.6
|
1.0
|
O
|
F:PHE196
|
4.7
|
33.9
|
1.0
|
O
|
F:VAL194
|
4.7
|
34.5
|
1.0
|
O
|
F:HOH889
|
4.7
|
40.6
|
1.0
|
CA
|
F:HIS197
|
4.8
|
33.3
|
1.0
|
N
|
F:PHE196
|
4.8
|
30.0
|
1.0
|
|
Reference:
P.M.Lombardi,
H.D.Angell,
D.A.Whittington,
E.F.Flynn,
K.R.Rajashankar,
D.W.Christianson.
Structure of Prokaryotic Polyamine Deacetylase Reveals Evolutionary Functional Relationships with Eukaryotic Histone Deacetylases . Biochemistry V. 50 1808 2011.
ISSN: ISSN 0006-2960
PubMed: 21268586
DOI: 10.1021/BI101859K
Page generated: Mon Aug 12 09:10:47 2024
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