Potassium in PDB 8szt: Structure of KDAC1 From Acinetobacter Baumannii
Protein crystallography data
The structure of Structure of KDAC1 From Acinetobacter Baumannii, PDB code: 8szt
was solved by
P.R.Watson,
D.W.Christianson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
60.51 /
2.50
|
|
Space group
|
C 2 2 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
113.949,
181.689,
155.33,
90,
90,
90
|
|
R / Rfree (%)
|
20.1 /
26.2
|
Other elements in 8szt:
The structure of Structure of KDAC1 From Acinetobacter Baumannii also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of KDAC1 From Acinetobacter Baumannii
(pdb code 8szt). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the
Structure of KDAC1 From Acinetobacter Baumannii, PDB code: 8szt:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 8szt
Go back to
Potassium Binding Sites List in 8szt
Potassium binding site 1 out
of 8 in the Structure of KDAC1 From Acinetobacter Baumannii
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structure of KDAC1 From Acinetobacter Baumannii within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K402
b:30.5
occ:1.00
|
O
|
B:ASP181
|
2.6
|
16.0
|
1.0
|
|
O
|
B:HIS183
|
2.9
|
22.6
|
1.0
|
|
O
|
B:ILE203
|
3.0
|
16.7
|
1.0
|
|
OG
|
B:SER202
|
3.0
|
19.8
|
1.0
|
|
O
|
B:ASP179
|
3.1
|
13.7
|
1.0
|
|
CG
|
B:ASP179
|
3.1
|
22.6
|
1.0
|
|
OD2
|
B:ASP179
|
3.2
|
25.6
|
1.0
|
|
OD1
|
B:ASP179
|
3.3
|
21.1
|
1.0
|
|
C
|
B:ASP179
|
3.6
|
14.9
|
1.0
|
|
C
|
B:ASP181
|
3.6
|
17.9
|
1.0
|
|
C
|
B:ILE203
|
3.7
|
18.3
|
1.0
|
|
CB
|
B:ASP179
|
3.8
|
15.6
|
1.0
|
|
N
|
B:ASP181
|
3.8
|
16.4
|
1.0
|
|
N
|
B:ILE203
|
3.9
|
16.8
|
1.0
|
|
C
|
B:HIS183
|
3.9
|
17.4
|
1.0
|
|
CB
|
B:SER202
|
4.0
|
19.1
|
1.0
|
|
CB
|
B:HIS204
|
4.0
|
18.3
|
1.0
|
|
CA
|
B:ASP181
|
4.1
|
18.1
|
1.0
|
|
CA
|
B:SER202
|
4.1
|
18.9
|
1.0
|
|
N
|
B:GLY185
|
4.2
|
18.2
|
1.0
|
|
C
|
B:TRP180
|
4.2
|
15.3
|
1.0
|
|
N
|
B:TRP180
|
4.2
|
14.3
|
1.0
|
|
CB
|
B:ASP181
|
4.3
|
17.7
|
1.0
|
|
C
|
B:SER202
|
4.3
|
19.6
|
1.0
|
|
CA
|
B:TRP180
|
4.3
|
16.5
|
1.0
|
|
CA
|
B:ASP179
|
4.3
|
17.2
|
1.0
|
|
N
|
B:HIS204
|
4.4
|
18.8
|
1.0
|
|
CA
|
B:HIS204
|
4.4
|
17.8
|
1.0
|
|
CA
|
B:ILE203
|
4.5
|
15.2
|
1.0
|
|
CA
|
B:HIS184
|
4.5
|
21.4
|
1.0
|
|
CE1
|
B:HIS143
|
4.5
|
21.2
|
1.0
|
|
N
|
B:HIS183
|
4.5
|
14.7
|
1.0
|
|
ND1
|
B:HIS143
|
4.6
|
20.6
|
1.0
|
|
N
|
B:HIS184
|
4.6
|
20.7
|
1.0
|
|
C
|
B:HIS184
|
4.7
|
19.5
|
1.0
|
|
N
|
B:VAL182
|
4.8
|
17.1
|
1.0
|
|
ND1
|
B:HIS204
|
4.8
|
23.3
|
1.0
|
|
CG
|
B:HIS204
|
4.8
|
21.8
|
1.0
|
|
C
|
B:VAL182
|
4.9
|
15.6
|
1.0
|
|
CA
|
B:HIS183
|
4.9
|
18.4
|
1.0
|
|
O
|
B:HOH501
|
4.9
|
9.2
|
1.0
|
|
O
|
B:TRP180
|
4.9
|
13.5
|
1.0
|
|
Potassium binding site 2 out
of 8 in 8szt
Go back to
Potassium Binding Sites List in 8szt
Potassium binding site 2 out
of 8 in the Structure of KDAC1 From Acinetobacter Baumannii
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structure of KDAC1 From Acinetobacter Baumannii within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K403
b:23.4
occ:1.00
|
O
|
B:HOH508
|
2.5
|
19.8
|
1.0
|
|
O
|
B:TRP192
|
2.6
|
22.6
|
1.0
|
|
O
|
B:ASP195
|
2.7
|
26.7
|
1.0
|
|
O
|
B:VAL198
|
2.8
|
17.4
|
1.0
|
|
O
|
B:TYR227
|
2.9
|
19.6
|
1.0
|
|
O
|
B:HOH502
|
3.0
|
19.0
|
1.0
|
|
CB
|
B:TRP192
|
3.4
|
15.8
|
1.0
|
|
C
|
B:TRP192
|
3.5
|
23.5
|
1.0
|
|
OG1
|
B:THR200
|
3.6
|
18.0
|
1.0
|
|
C
|
B:TYR227
|
3.8
|
24.7
|
1.0
|
|
C
|
B:ASP195
|
3.9
|
26.2
|
1.0
|
|
C
|
B:VAL198
|
3.9
|
18.8
|
1.0
|
|
CG2
|
B:THR200
|
4.0
|
18.5
|
1.0
|
|
CB
|
B:TYR227
|
4.1
|
24.0
|
1.0
|
|
CA
|
B:TRP192
|
4.1
|
19.9
|
1.0
|
|
N
|
B:THR200
|
4.3
|
15.1
|
1.0
|
|
CB
|
B:THR200
|
4.4
|
18.6
|
1.0
|
|
N
|
B:TRP193
|
4.6
|
25.6
|
1.0
|
|
N
|
B:ASP195
|
4.6
|
25.9
|
1.0
|
|
CA
|
B:TYR227
|
4.6
|
23.8
|
1.0
|
|
N
|
B:ASN228
|
4.7
|
23.0
|
1.0
|
|
CA
|
B:ASP195
|
4.7
|
27.6
|
1.0
|
|
CG
|
B:TRP192
|
4.7
|
18.1
|
1.0
|
|
O
|
B:TRP193
|
4.8
|
23.1
|
1.0
|
|
CA
|
B:LEU199
|
4.8
|
18.2
|
1.0
|
|
N
|
B:LEU199
|
4.8
|
19.1
|
1.0
|
|
CA
|
B:TRP193
|
4.8
|
23.7
|
1.0
|
|
CB
|
B:ASN228
|
4.8
|
22.8
|
1.0
|
|
CA
|
B:VAL198
|
4.9
|
20.1
|
1.0
|
|
C
|
B:TRP193
|
4.9
|
27.2
|
1.0
|
|
N
|
B:SER196
|
4.9
|
25.9
|
1.0
|
|
CB
|
B:ASP195
|
4.9
|
25.7
|
1.0
|
|
C
|
B:LEU199
|
4.9
|
17.2
|
1.0
|
|
CA
|
B:ASN228
|
5.0
|
26.2
|
1.0
|
|
CB
|
B:VAL198
|
5.0
|
26.6
|
1.0
|
|
N
|
B:VAL198
|
5.0
|
18.0
|
1.0
|
|
Potassium binding site 3 out
of 8 in 8szt
Go back to
Potassium Binding Sites List in 8szt
Potassium binding site 3 out
of 8 in the Structure of KDAC1 From Acinetobacter Baumannii
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Structure of KDAC1 From Acinetobacter Baumannii within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K402
b:23.8
occ:1.00
|
O
|
A:ASP181
|
2.6
|
20.6
|
1.0
|
|
O
|
A:HIS183
|
2.8
|
16.9
|
1.0
|
|
OG
|
A:SER202
|
3.0
|
14.7
|
1.0
|
|
O
|
A:ASP179
|
3.0
|
12.4
|
1.0
|
|
O
|
A:ILE203
|
3.0
|
17.8
|
1.0
|
|
CG
|
A:ASP179
|
3.2
|
31.6
|
1.0
|
|
OD1
|
A:ASP179
|
3.4
|
32.8
|
1.0
|
|
OD2
|
A:ASP179
|
3.4
|
26.1
|
1.0
|
|
C
|
A:ASP179
|
3.6
|
17.1
|
1.0
|
|
C
|
A:ASP181
|
3.6
|
16.0
|
1.0
|
|
C
|
A:ILE203
|
3.8
|
16.3
|
1.0
|
|
N
|
A:ASP181
|
3.8
|
13.9
|
1.0
|
|
CB
|
A:ASP179
|
3.8
|
18.3
|
1.0
|
|
N
|
A:ILE203
|
3.8
|
12.6
|
1.0
|
|
C
|
A:HIS183
|
3.9
|
14.9
|
1.0
|
|
CB
|
A:SER202
|
3.9
|
15.0
|
1.0
|
|
CB
|
A:HIS204
|
4.0
|
13.4
|
1.0
|
|
C
|
A:TRP180
|
4.0
|
14.7
|
1.0
|
|
CA
|
A:SER202
|
4.1
|
16.5
|
1.0
|
|
CA
|
A:ASP181
|
4.1
|
16.4
|
1.0
|
|
N
|
A:TRP180
|
4.1
|
16.4
|
1.0
|
|
CA
|
A:TRP180
|
4.2
|
19.3
|
1.0
|
|
CB
|
A:ASP181
|
4.2
|
18.8
|
1.0
|
|
N
|
A:GLY185
|
4.2
|
12.7
|
1.0
|
|
C
|
A:SER202
|
4.2
|
17.5
|
1.0
|
|
CA
|
A:ASP179
|
4.3
|
17.9
|
1.0
|
|
CA
|
A:HIS184
|
4.4
|
15.5
|
1.0
|
|
CA
|
A:HIS204
|
4.5
|
16.1
|
1.0
|
|
N
|
A:HIS204
|
4.5
|
13.4
|
1.0
|
|
N
|
A:HIS183
|
4.5
|
17.6
|
1.0
|
|
CA
|
A:ILE203
|
4.5
|
17.5
|
1.0
|
|
N
|
A:HIS184
|
4.6
|
15.6
|
1.0
|
|
O
|
A:TRP180
|
4.7
|
14.3
|
1.0
|
|
C
|
A:HIS184
|
4.7
|
14.6
|
1.0
|
|
ND1
|
A:HIS143
|
4.8
|
25.0
|
1.0
|
|
ND1
|
A:HIS204
|
4.8
|
20.5
|
1.0
|
|
C
|
A:VAL182
|
4.8
|
16.9
|
1.0
|
|
N
|
A:VAL182
|
4.8
|
17.9
|
1.0
|
|
CE1
|
A:HIS143
|
4.8
|
23.5
|
1.0
|
|
CG
|
A:HIS204
|
4.8
|
20.7
|
1.0
|
|
CA
|
A:HIS183
|
4.9
|
16.5
|
1.0
|
|
Potassium binding site 4 out
of 8 in 8szt
Go back to
Potassium Binding Sites List in 8szt
Potassium binding site 4 out
of 8 in the Structure of KDAC1 From Acinetobacter Baumannii
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Structure of KDAC1 From Acinetobacter Baumannii within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K403
b:22.9
occ:1.00
|
O
|
A:TRP192
|
2.6
|
11.7
|
1.0
|
|
O
|
A:VAL198
|
2.7
|
18.0
|
1.0
|
|
O
|
A:TYR227
|
2.8
|
21.0
|
1.0
|
|
O
|
A:ASP195
|
2.9
|
27.5
|
1.0
|
|
O
|
A:HOH507
|
2.9
|
21.4
|
1.0
|
|
C
|
A:TRP192
|
3.6
|
17.4
|
1.0
|
|
CB
|
A:TRP192
|
3.6
|
14.4
|
1.0
|
|
C
|
A:TYR227
|
3.8
|
25.2
|
1.0
|
|
OG1
|
A:THR200
|
3.9
|
22.9
|
1.0
|
|
C
|
A:VAL198
|
3.9
|
18.0
|
1.0
|
|
C
|
A:ASP195
|
4.1
|
25.8
|
1.0
|
|
CG2
|
A:THR200
|
4.1
|
13.2
|
1.0
|
|
CB
|
A:TYR227
|
4.1
|
21.4
|
1.0
|
|
CA
|
A:TRP192
|
4.2
|
20.3
|
1.0
|
|
N
|
A:THR200
|
4.3
|
15.6
|
1.0
|
|
N
|
A:TRP193
|
4.5
|
18.5
|
1.0
|
|
N
|
A:ASN228
|
4.5
|
18.6
|
1.0
|
|
CB
|
A:THR200
|
4.6
|
13.5
|
1.0
|
|
CA
|
A:TYR227
|
4.6
|
24.5
|
1.0
|
|
CA
|
A:LEU199
|
4.6
|
21.1
|
1.0
|
|
O
|
A:TRP193
|
4.6
|
22.1
|
1.0
|
|
N
|
A:ASP195
|
4.6
|
28.4
|
1.0
|
|
CA
|
A:TRP193
|
4.7
|
20.5
|
1.0
|
|
C
|
A:TRP193
|
4.7
|
24.0
|
1.0
|
|
CB
|
A:ASN228
|
4.7
|
21.0
|
1.0
|
|
N
|
A:LEU199
|
4.7
|
14.7
|
1.0
|
|
CA
|
A:ASN228
|
4.8
|
20.2
|
1.0
|
|
C
|
A:LEU199
|
4.8
|
17.2
|
1.0
|
|
CA
|
A:ASP195
|
4.8
|
22.4
|
1.0
|
|
CG
|
A:TRP192
|
4.9
|
16.6
|
1.0
|
|
O
|
A:GLY224
|
4.9
|
34.2
|
1.0
|
|
CA
|
A:VAL198
|
4.9
|
24.8
|
1.0
|
|
Potassium binding site 5 out
of 8 in 8szt
Go back to
Potassium Binding Sites List in 8szt
Potassium binding site 5 out
of 8 in the Structure of KDAC1 From Acinetobacter Baumannii
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Structure of KDAC1 From Acinetobacter Baumannii within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K402
b:25.8
occ:1.00
|
O
|
C:ASP181
|
2.6
|
20.1
|
1.0
|
|
O
|
C:ILE203
|
2.8
|
17.5
|
1.0
|
|
O
|
C:HIS183
|
2.9
|
21.4
|
1.0
|
|
O
|
C:ASP179
|
2.9
|
18.2
|
1.0
|
|
OD2
|
C:ASP179
|
3.0
|
23.8
|
1.0
|
|
OG
|
C:SER202
|
3.1
|
17.3
|
1.0
|
|
CG
|
C:ASP179
|
3.1
|
25.8
|
1.0
|
|
OD1
|
C:ASP179
|
3.1
|
23.1
|
1.0
|
|
C
|
C:ASP179
|
3.6
|
19.4
|
1.0
|
|
C
|
C:ASP181
|
3.6
|
16.9
|
1.0
|
|
C
|
C:ILE203
|
3.7
|
23.7
|
1.0
|
|
CB
|
C:SER202
|
3.8
|
19.9
|
1.0
|
|
N
|
C:ASP181
|
3.8
|
15.9
|
1.0
|
|
C
|
C:HIS183
|
3.9
|
16.5
|
1.0
|
|
CB
|
C:HIS204
|
3.9
|
22.6
|
1.0
|
|
N
|
C:ILE203
|
4.0
|
16.4
|
1.0
|
|
CA
|
C:ASP181
|
4.0
|
17.3
|
1.0
|
|
C
|
C:TRP180
|
4.1
|
16.9
|
1.0
|
|
CA
|
C:SER202
|
4.1
|
19.2
|
1.0
|
|
CB
|
C:ASP181
|
4.1
|
18.4
|
1.0
|
|
N
|
C:TRP180
|
4.1
|
18.8
|
1.0
|
|
N
|
C:GLY185
|
4.1
|
21.3
|
1.0
|
|
CB
|
C:ASP179
|
4.1
|
22.7
|
1.0
|
|
CA
|
C:TRP180
|
4.2
|
16.6
|
1.0
|
|
C
|
C:SER202
|
4.2
|
22.7
|
1.0
|
|
CA
|
C:HIS184
|
4.4
|
19.8
|
1.0
|
|
CA
|
C:ASP179
|
4.4
|
20.3
|
1.0
|
|
CA
|
C:HIS204
|
4.5
|
18.7
|
1.0
|
|
N
|
C:HIS184
|
4.5
|
21.6
|
1.0
|
|
N
|
C:HIS183
|
4.5
|
15.0
|
1.0
|
|
CA
|
C:ILE203
|
4.5
|
21.4
|
1.0
|
|
N
|
C:HIS204
|
4.5
|
18.7
|
1.0
|
|
C
|
C:HIS184
|
4.5
|
20.6
|
1.0
|
|
ND1
|
C:HIS143
|
4.7
|
18.8
|
1.0
|
|
CE1
|
C:HIS143
|
4.7
|
18.1
|
1.0
|
|
ND1
|
C:HIS204
|
4.7
|
25.1
|
1.0
|
|
N
|
C:VAL182
|
4.7
|
16.9
|
1.0
|
|
O
|
C:HOH504
|
4.7
|
17.5
|
1.0
|
|
O
|
C:TRP180
|
4.8
|
18.2
|
1.0
|
|
CG
|
C:HIS204
|
4.8
|
24.1
|
1.0
|
|
CA
|
C:HIS183
|
4.9
|
14.2
|
1.0
|
|
C
|
C:VAL182
|
4.9
|
16.2
|
1.0
|
|
CA
|
C:GLY185
|
5.0
|
19.2
|
1.0
|
|
Potassium binding site 6 out
of 8 in 8szt
Go back to
Potassium Binding Sites List in 8szt
Potassium binding site 6 out
of 8 in the Structure of KDAC1 From Acinetobacter Baumannii
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Structure of KDAC1 From Acinetobacter Baumannii within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K403
b:23.9
occ:1.00
|
O
|
C:TYR227
|
2.6
|
21.3
|
1.0
|
|
O
|
C:HOH507
|
2.7
|
19.1
|
1.0
|
|
O
|
C:VAL198
|
2.7
|
17.9
|
1.0
|
|
O
|
C:TRP192
|
2.7
|
18.9
|
1.0
|
|
O
|
C:ASP195
|
2.8
|
31.6
|
1.0
|
|
O
|
C:HOH508
|
2.8
|
13.1
|
1.0
|
|
C
|
C:TYR227
|
3.6
|
21.5
|
1.0
|
|
CB
|
C:TRP192
|
3.6
|
19.9
|
1.0
|
|
C
|
C:TRP192
|
3.7
|
23.9
|
1.0
|
|
C
|
C:VAL198
|
3.9
|
22.4
|
1.0
|
|
OG1
|
C:THR200
|
3.9
|
17.8
|
1.0
|
|
CB
|
C:TYR227
|
4.0
|
19.1
|
1.0
|
|
C
|
C:ASP195
|
4.0
|
30.0
|
1.0
|
|
CG2
|
C:THR200
|
4.1
|
19.6
|
1.0
|
|
N
|
C:THR200
|
4.2
|
21.1
|
1.0
|
|
CA
|
C:TRP192
|
4.3
|
22.4
|
1.0
|
|
CA
|
C:TYR227
|
4.4
|
18.5
|
1.0
|
|
N
|
C:ASN228
|
4.4
|
18.5
|
1.0
|
|
CB
|
C:THR200
|
4.6
|
16.5
|
1.0
|
|
N
|
C:ASP195
|
4.6
|
27.5
|
1.0
|
|
CA
|
C:LEU199
|
4.6
|
19.9
|
1.0
|
|
N
|
C:TRP193
|
4.7
|
20.6
|
1.0
|
|
CB
|
C:ASN228
|
4.7
|
23.5
|
1.0
|
|
N
|
C:LEU199
|
4.7
|
23.8
|
1.0
|
|
CA
|
C:ASN228
|
4.8
|
14.9
|
1.0
|
|
CA
|
C:ASP195
|
4.8
|
30.2
|
1.0
|
|
C
|
C:LEU199
|
4.8
|
22.8
|
1.0
|
|
O
|
C:TRP193
|
4.9
|
17.2
|
1.0
|
|
CA
|
C:VAL198
|
4.9
|
17.1
|
1.0
|
|
CG
|
C:TRP192
|
4.9
|
16.7
|
1.0
|
|
O
|
C:GLY224
|
4.9
|
25.4
|
1.0
|
|
CA
|
C:TRP193
|
4.9
|
19.3
|
1.0
|
|
C
|
C:TRP193
|
4.9
|
26.3
|
1.0
|
|
CB
|
C:VAL198
|
4.9
|
22.7
|
1.0
|
|
N
|
C:SER196
|
5.0
|
27.1
|
1.0
|
|
Potassium binding site 7 out
of 8 in 8szt
Go back to
Potassium Binding Sites List in 8szt
Potassium binding site 7 out
of 8 in the Structure of KDAC1 From Acinetobacter Baumannii
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Structure of KDAC1 From Acinetobacter Baumannii within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K402
b:29.2
occ:1.00
|
O
|
D:ASP181
|
2.6
|
17.9
|
1.0
|
|
OG
|
D:SER202
|
2.7
|
12.9
|
1.0
|
|
O
|
D:ILE203
|
3.0
|
13.2
|
1.0
|
|
O
|
D:ASP179
|
3.1
|
10.7
|
1.0
|
|
O
|
D:HIS183
|
3.1
|
12.8
|
1.0
|
|
OD2
|
D:ASP179
|
3.3
|
14.4
|
1.0
|
|
CG
|
D:ASP179
|
3.4
|
20.1
|
1.0
|
|
C
|
D:ASP181
|
3.6
|
16.7
|
1.0
|
|
C
|
D:ASP179
|
3.7
|
16.1
|
1.0
|
|
N
|
D:ASP181
|
3.7
|
14.2
|
1.0
|
|
OD1
|
D:ASP179
|
3.7
|
30.8
|
1.0
|
|
C
|
D:ILE203
|
3.7
|
15.8
|
1.0
|
|
CB
|
D:SER202
|
3.8
|
13.3
|
1.0
|
|
N
|
D:ILE203
|
3.8
|
11.4
|
1.0
|
|
CB
|
D:HIS204
|
3.9
|
14.4
|
1.0
|
|
C
|
D:HIS183
|
4.0
|
17.2
|
1.0
|
|
N
|
D:GLY185
|
4.0
|
14.3
|
1.0
|
|
CB
|
D:ASP179
|
4.0
|
14.6
|
1.0
|
|
CA
|
D:SER202
|
4.0
|
14.7
|
1.0
|
|
CA
|
D:ASP181
|
4.1
|
15.1
|
1.0
|
|
C
|
D:TRP180
|
4.1
|
17.2
|
1.0
|
|
C
|
D:SER202
|
4.2
|
15.6
|
1.0
|
|
N
|
D:TRP180
|
4.3
|
14.6
|
1.0
|
|
CB
|
D:ASP181
|
4.3
|
13.2
|
1.0
|
|
CA
|
D:TRP180
|
4.3
|
13.6
|
1.0
|
|
CA
|
D:HIS184
|
4.3
|
16.7
|
1.0
|
|
ND1
|
D:HIS204
|
4.4
|
20.4
|
1.0
|
|
CA
|
D:HIS204
|
4.4
|
15.9
|
1.0
|
|
N
|
D:HIS204
|
4.5
|
16.4
|
1.0
|
|
CA
|
D:ILE203
|
4.5
|
14.4
|
1.0
|
|
CA
|
D:ASP179
|
4.5
|
17.3
|
1.0
|
|
C
|
D:HIS184
|
4.6
|
19.2
|
1.0
|
|
N
|
D:HIS183
|
4.6
|
14.2
|
1.0
|
|
N
|
D:HIS184
|
4.6
|
14.1
|
1.0
|
|
CG
|
D:HIS204
|
4.6
|
17.5
|
1.0
|
|
ND1
|
D:HIS143
|
4.7
|
13.0
|
1.0
|
|
N
|
D:VAL182
|
4.8
|
14.1
|
1.0
|
|
CE1
|
D:HIS143
|
4.8
|
17.4
|
1.0
|
|
CA
|
D:GLY185
|
4.9
|
12.2
|
1.0
|
|
O
|
D:HOH501
|
4.9
|
10.0
|
1.0
|
|
C
|
D:VAL182
|
4.9
|
17.2
|
1.0
|
|
O
|
D:TRP180
|
4.9
|
20.3
|
1.0
|
|
CA
|
D:HIS183
|
5.0
|
13.3
|
1.0
|
|
Potassium binding site 8 out
of 8 in 8szt
Go back to
Potassium Binding Sites List in 8szt
Potassium binding site 8 out
of 8 in the Structure of KDAC1 From Acinetobacter Baumannii
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of Structure of KDAC1 From Acinetobacter Baumannii within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K403
b:21.4
occ:1.00
|
O
|
D:TRP192
|
2.5
|
16.4
|
1.0
|
|
O
|
D:HOH503
|
2.7
|
18.7
|
1.0
|
|
O
|
D:VAL198
|
2.7
|
15.0
|
1.0
|
|
O
|
D:ASP195
|
2.9
|
29.8
|
1.0
|
|
O
|
D:TYR227
|
3.0
|
20.4
|
1.0
|
|
O
|
D:HOH505
|
3.2
|
18.6
|
1.0
|
|
C
|
D:TRP192
|
3.5
|
19.2
|
1.0
|
|
CB
|
D:TRP192
|
3.6
|
13.8
|
1.0
|
|
C
|
D:TYR227
|
3.9
|
22.9
|
1.0
|
|
C
|
D:VAL198
|
3.9
|
17.0
|
1.0
|
|
OG1
|
D:THR200
|
4.0
|
19.0
|
1.0
|
|
C
|
D:ASP195
|
4.0
|
23.1
|
1.0
|
|
CG2
|
D:THR200
|
4.0
|
22.0
|
1.0
|
|
CB
|
D:TYR227
|
4.1
|
15.4
|
1.0
|
|
CA
|
D:TRP192
|
4.2
|
17.2
|
1.0
|
|
N
|
D:THR200
|
4.4
|
15.7
|
1.0
|
|
N
|
D:ASP195
|
4.5
|
22.2
|
1.0
|
|
N
|
D:TRP193
|
4.6
|
18.1
|
1.0
|
|
CB
|
D:THR200
|
4.6
|
17.7
|
1.0
|
|
N
|
D:ASN228
|
4.6
|
19.4
|
1.0
|
|
CA
|
D:TYR227
|
4.6
|
17.1
|
1.0
|
|
CA
|
D:LEU199
|
4.6
|
17.7
|
1.0
|
|
O
|
D:TRP193
|
4.7
|
17.9
|
1.0
|
|
CB
|
D:ASN228
|
4.7
|
19.0
|
1.0
|
|
CA
|
D:ASP195
|
4.7
|
22.1
|
1.0
|
|
N
|
D:LEU199
|
4.8
|
16.4
|
1.0
|
|
C
|
D:TRP193
|
4.8
|
20.1
|
1.0
|
|
CA
|
D:TRP193
|
4.8
|
19.4
|
1.0
|
|
CG
|
D:TRP192
|
4.8
|
19.1
|
1.0
|
|
CA
|
D:ASN228
|
4.9
|
16.5
|
1.0
|
|
C
|
D:LEU199
|
4.9
|
20.5
|
1.0
|
|
CA
|
D:VAL198
|
4.9
|
21.0
|
1.0
|
|
O
|
D:GLY224
|
4.9
|
22.3
|
1.0
|
|
CB
|
D:ASP195
|
5.0
|
20.0
|
1.0
|
|
Reference:
P.R.Watson,
D.W.Christianson.
Structure and Function of KDAC1, A Class II Deacetylase From the Multidrug-Resistant Pathogen Acinetobacter Baumannii. Biochemistry 2023.
ISSN: ISSN 0006-2960
PubMed: 37624144
DOI: 10.1021/ACS.BIOCHEM.3C00288
Page generated: Tue Aug 13 00:54:07 2024
|
