Potassium in PDB 1pvn: The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
Enzymatic activity of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
All present enzymatic activity of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp:
1.1.1.205;
Protein crystallography data
The structure of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp, PDB code: 1pvn
was solved by
L.Gan,
M.Seyedsayamdost,
S.Shuto,
A.Matsuda,
G.A.Petsko,
L.Hedstrom,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.71 /
2.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
96.754,
112.566,
159.756,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.6 /
22.2
|
Potassium Binding Sites:
The binding sites of Potassium atom in the The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
(pdb code 1pvn). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the
The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp, PDB code: 1pvn:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 1pvn
Go back to
Potassium Binding Sites List in 1pvn
Potassium binding site 1 out
of 8 in the The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K981
b:13.0
occ:1.00
|
O
|
D:GLY316
|
2.6
|
14.7
|
1.0
|
O
|
D:GLY314
|
2.7
|
17.4
|
1.0
|
O
|
A:GLU485
|
2.7
|
15.2
|
1.0
|
O
|
D:CYS319
|
2.7
|
12.9
|
1.0
|
O
|
A:GLY487
|
3.0
|
19.0
|
1.0
|
O
|
A:GLY486
|
3.4
|
17.9
|
1.0
|
C
|
A:GLY486
|
3.6
|
17.3
|
1.0
|
O
|
A:HOH1034
|
3.7
|
19.9
|
1.0
|
C
|
D:CYS319
|
3.7
|
13.8
|
1.0
|
C
|
D:GLY316
|
3.7
|
14.5
|
1.0
|
C
|
D:GLY314
|
3.8
|
16.0
|
1.0
|
C
|
A:GLY487
|
3.8
|
19.1
|
1.0
|
C
|
D:GLY315
|
3.8
|
15.5
|
1.0
|
C
|
A:GLU485
|
3.8
|
15.0
|
1.0
|
CB
|
D:CYS319
|
3.9
|
13.3
|
1.0
|
CD2
|
A:HIS489
|
4.0
|
15.8
|
1.0
|
N
|
D:GLY316
|
4.0
|
14.8
|
1.0
|
O
|
D:GLY315
|
4.0
|
13.8
|
1.0
|
CA
|
A:GLY486
|
4.1
|
15.7
|
1.0
|
N
|
A:GLY487
|
4.1
|
17.4
|
1.0
|
CA
|
D:CYS319
|
4.1
|
14.0
|
1.0
|
N
|
D:CYS319
|
4.1
|
13.0
|
1.0
|
NE2
|
A:HIS489
|
4.2
|
16.1
|
1.0
|
CA
|
D:GLY315
|
4.2
|
14.9
|
1.0
|
CA
|
A:GLY487
|
4.4
|
18.3
|
1.0
|
CA
|
D:GLY316
|
4.4
|
14.7
|
1.0
|
N
|
A:GLY486
|
4.4
|
14.9
|
1.0
|
N
|
D:GLY315
|
4.4
|
15.6
|
1.0
|
N
|
A:ALA488
|
4.6
|
19.0
|
1.0
|
N
|
D:SER317
|
4.7
|
14.5
|
1.0
|
SG
|
D:CYS319
|
4.7
|
16.8
|
1.0
|
N
|
D:ILE320
|
4.8
|
13.1
|
1.0
|
CA
|
A:ALA488
|
4.8
|
18.4
|
1.0
|
CA
|
D:GLY314
|
4.8
|
15.7
|
1.0
|
C
|
D:SER317
|
4.8
|
15.7
|
1.0
|
O
|
D:SER317
|
4.9
|
18.3
|
1.0
|
CA
|
D:SER317
|
4.9
|
15.7
|
1.0
|
|
Potassium binding site 2 out
of 8 in 1pvn
Go back to
Potassium Binding Sites List in 1pvn
Potassium binding site 2 out
of 8 in the The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K987
b:18.0
occ:1.00
|
O
|
B:GLY20
|
2.5
|
16.1
|
1.0
|
OD2
|
A:ASP264
|
2.6
|
21.8
|
1.0
|
OG
|
B:SER22
|
2.6
|
19.6
|
1.0
|
O
|
B:ASN460
|
2.7
|
16.3
|
1.0
|
O
|
A:PHE266
|
2.7
|
12.9
|
1.0
|
OD1
|
A:ASP264
|
3.0
|
15.1
|
1.0
|
CG
|
A:ASP264
|
3.2
|
17.6
|
1.0
|
CB
|
B:SER22
|
3.6
|
18.9
|
1.0
|
N
|
B:SER22
|
3.6
|
16.8
|
1.0
|
O
|
A:HOH1079
|
3.6
|
27.9
|
1.0
|
C
|
B:GLY20
|
3.7
|
16.4
|
1.0
|
C
|
B:ASN460
|
3.7
|
18.2
|
1.0
|
C
|
A:PHE266
|
3.7
|
15.9
|
1.0
|
CB
|
A:PHE266
|
3.8
|
14.2
|
1.0
|
CB
|
B:PRO19
|
4.0
|
17.3
|
1.0
|
CA
|
B:ASN460
|
4.1
|
17.4
|
1.0
|
C
|
B:LEU21
|
4.1
|
17.6
|
1.0
|
CA
|
B:SER22
|
4.1
|
18.1
|
1.0
|
N
|
B:GLY20
|
4.2
|
18.1
|
1.0
|
CA
|
A:PHE266
|
4.2
|
14.7
|
1.0
|
CA
|
B:LEU21
|
4.3
|
18.0
|
1.0
|
N
|
B:LEU21
|
4.5
|
18.0
|
1.0
|
N
|
A:PHE266
|
4.5
|
14.9
|
1.0
|
C
|
B:PRO19
|
4.6
|
17.2
|
1.0
|
CG
|
A:PHE266
|
4.6
|
16.0
|
1.0
|
CB
|
A:ASP264
|
4.6
|
15.8
|
1.0
|
CA
|
B:GLY20
|
4.6
|
17.2
|
1.0
|
CA
|
B:PRO19
|
4.7
|
17.2
|
1.0
|
O
|
B:CYS459
|
4.7
|
14.6
|
1.0
|
CB
|
B:ASN460
|
4.7
|
17.7
|
1.0
|
N
|
A:SER267
|
4.8
|
16.5
|
1.0
|
O
|
B:LEU21
|
4.9
|
16.2
|
1.0
|
N
|
B:CYS461
|
4.9
|
18.0
|
1.0
|
O
|
A:HOH1047
|
4.9
|
14.7
|
1.0
|
CB
|
A:SER267
|
5.0
|
20.6
|
1.0
|
|
Potassium binding site 3 out
of 8 in 1pvn
Go back to
Potassium Binding Sites List in 1pvn
Potassium binding site 3 out
of 8 in the The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K988
b:16.1
occ:1.00
|
O
|
A:GLY20
|
2.4
|
14.4
|
1.0
|
OD2
|
D:ASP264
|
2.5
|
23.5
|
1.0
|
OG
|
A:SER22
|
2.5
|
17.8
|
1.0
|
O
|
A:ASN460
|
2.6
|
14.1
|
1.0
|
O
|
D:PHE266
|
2.8
|
15.7
|
1.0
|
OD1
|
D:ASP264
|
3.1
|
20.1
|
1.0
|
CG
|
D:ASP264
|
3.2
|
20.5
|
1.0
|
CB
|
A:SER22
|
3.5
|
15.7
|
1.0
|
N
|
A:SER22
|
3.5
|
16.3
|
1.0
|
C
|
A:GLY20
|
3.6
|
14.8
|
1.0
|
O
|
D:HOH1202
|
3.6
|
23.9
|
1.0
|
C
|
A:ASN460
|
3.6
|
17.1
|
1.0
|
C
|
D:PHE266
|
3.8
|
17.1
|
1.0
|
CB
|
D:PHE266
|
3.9
|
14.3
|
1.0
|
C
|
A:LEU21
|
4.0
|
17.0
|
1.0
|
CB
|
A:PRO19
|
4.0
|
16.7
|
1.0
|
CA
|
A:ASN460
|
4.0
|
15.8
|
1.0
|
CA
|
A:SER22
|
4.0
|
18.1
|
1.0
|
N
|
A:GLY20
|
4.2
|
15.2
|
1.0
|
CA
|
A:LEU21
|
4.3
|
16.2
|
1.0
|
CA
|
D:PHE266
|
4.3
|
15.6
|
1.0
|
N
|
A:LEU21
|
4.4
|
15.6
|
1.0
|
C
|
A:PRO19
|
4.6
|
15.4
|
1.0
|
N
|
D:PHE266
|
4.6
|
16.7
|
1.0
|
CA
|
A:GLY20
|
4.6
|
14.8
|
1.0
|
CB
|
D:ASP264
|
4.6
|
16.9
|
1.0
|
O
|
A:CYS459
|
4.6
|
13.9
|
1.0
|
CG
|
D:PHE266
|
4.7
|
14.8
|
1.0
|
CB
|
A:ASN460
|
4.7
|
15.7
|
1.0
|
CA
|
A:PRO19
|
4.8
|
15.5
|
1.0
|
O
|
A:LEU21
|
4.8
|
16.0
|
1.0
|
N
|
A:CYS461
|
4.8
|
17.0
|
1.0
|
N
|
D:SER267
|
4.9
|
16.0
|
1.0
|
O
|
D:HOH1002
|
4.9
|
10.8
|
1.0
|
|
Potassium binding site 4 out
of 8 in 1pvn
Go back to
Potassium Binding Sites List in 1pvn
Potassium binding site 4 out
of 8 in the The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K982
b:15.4
occ:1.00
|
O
|
A:GLY316
|
2.6
|
13.6
|
1.0
|
O
|
A:CYS319
|
2.6
|
16.4
|
1.0
|
O
|
B:GLY487
|
2.6
|
20.2
|
1.0
|
O
|
A:GLY314
|
2.7
|
17.9
|
1.0
|
O
|
B:GLU485
|
2.7
|
19.8
|
1.0
|
O
|
B:GLY486
|
2.9
|
21.4
|
1.0
|
C
|
B:GLY486
|
3.1
|
21.2
|
1.0
|
C
|
B:GLY487
|
3.3
|
21.1
|
1.0
|
N
|
B:GLY487
|
3.6
|
21.7
|
1.0
|
C
|
A:CYS319
|
3.6
|
17.4
|
1.0
|
O
|
B:HOH1004
|
3.7
|
24.2
|
1.0
|
C
|
A:GLY316
|
3.7
|
13.4
|
1.0
|
C
|
B:GLU485
|
3.8
|
19.0
|
1.0
|
CA
|
B:GLY486
|
3.8
|
19.7
|
1.0
|
C
|
A:GLY314
|
3.8
|
16.6
|
1.0
|
CA
|
B:GLY487
|
3.8
|
21.9
|
1.0
|
CB
|
A:CYS319
|
3.9
|
17.5
|
1.0
|
C
|
A:GLY315
|
3.9
|
14.9
|
1.0
|
N
|
A:GLY316
|
4.0
|
12.8
|
1.0
|
CA
|
A:CYS319
|
4.1
|
18.0
|
1.0
|
O
|
A:GLY315
|
4.1
|
15.2
|
1.0
|
N
|
A:CYS319
|
4.1
|
17.1
|
1.0
|
CD2
|
B:HIS489
|
4.1
|
17.4
|
1.0
|
N
|
B:ALA488
|
4.1
|
21.0
|
1.0
|
N
|
B:GLY486
|
4.2
|
18.2
|
1.0
|
CA
|
A:GLY315
|
4.3
|
15.3
|
1.0
|
CA
|
A:GLY316
|
4.4
|
13.6
|
1.0
|
N
|
A:GLY315
|
4.5
|
15.8
|
1.0
|
CA
|
B:ALA488
|
4.5
|
21.0
|
1.0
|
NE2
|
B:HIS489
|
4.5
|
16.7
|
1.0
|
SG
|
A:CYS319
|
4.7
|
19.5
|
1.0
|
N
|
A:SER317
|
4.7
|
14.8
|
1.0
|
N
|
A:ILE320
|
4.7
|
15.8
|
1.0
|
CA
|
A:GLY314
|
4.8
|
17.2
|
1.0
|
C
|
A:SER317
|
4.8
|
16.3
|
1.0
|
O
|
A:SER317
|
4.9
|
16.2
|
1.0
|
CA
|
A:SER317
|
4.9
|
16.3
|
1.0
|
|
Potassium binding site 5 out
of 8 in 1pvn
Go back to
Potassium Binding Sites List in 1pvn
Potassium binding site 5 out
of 8 in the The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K986
b:19.3
occ:1.00
|
O
|
C:GLY20
|
2.4
|
16.7
|
1.0
|
OG
|
C:SER22
|
2.5
|
21.8
|
1.0
|
OD2
|
B:ASP264
|
2.5
|
24.4
|
1.0
|
O
|
C:ASN460
|
2.5
|
16.1
|
1.0
|
O
|
B:PHE266
|
2.7
|
13.8
|
1.0
|
OD1
|
B:ASP264
|
3.0
|
19.9
|
1.0
|
CG
|
B:ASP264
|
3.1
|
21.2
|
1.0
|
O
|
B:HOH1027
|
3.4
|
26.0
|
1.0
|
CB
|
C:SER22
|
3.5
|
20.3
|
1.0
|
N
|
C:SER22
|
3.5
|
18.9
|
1.0
|
C
|
C:ASN460
|
3.5
|
17.2
|
1.0
|
C
|
C:GLY20
|
3.6
|
16.3
|
1.0
|
C
|
B:PHE266
|
3.7
|
14.9
|
1.0
|
CB
|
B:PHE266
|
3.7
|
15.0
|
1.0
|
CA
|
C:ASN460
|
3.9
|
17.0
|
1.0
|
CB
|
C:PRO19
|
4.0
|
18.1
|
1.0
|
CA
|
C:SER22
|
4.0
|
19.6
|
1.0
|
C
|
C:LEU21
|
4.0
|
19.4
|
1.0
|
N
|
C:GLY20
|
4.2
|
17.0
|
1.0
|
CA
|
B:PHE266
|
4.2
|
14.6
|
1.0
|
CA
|
C:LEU21
|
4.3
|
18.6
|
1.0
|
N
|
C:LEU21
|
4.4
|
16.7
|
1.0
|
N
|
B:PHE266
|
4.5
|
14.3
|
1.0
|
O
|
C:CYS459
|
4.6
|
16.5
|
1.0
|
CG
|
B:PHE266
|
4.6
|
16.1
|
1.0
|
C
|
C:PRO19
|
4.6
|
17.0
|
1.0
|
CB
|
B:ASP264
|
4.6
|
18.5
|
1.0
|
CA
|
C:GLY20
|
4.6
|
16.5
|
1.0
|
CB
|
C:ASN460
|
4.7
|
17.2
|
1.0
|
CA
|
C:PRO19
|
4.7
|
17.3
|
1.0
|
N
|
C:CYS461
|
4.7
|
16.5
|
1.0
|
O
|
C:LEU21
|
4.8
|
19.7
|
1.0
|
N
|
B:SER267
|
4.8
|
14.6
|
1.0
|
O
|
B:HOH1003
|
4.9
|
14.9
|
1.0
|
|
Potassium binding site 6 out
of 8 in 1pvn
Go back to
Potassium Binding Sites List in 1pvn
Potassium binding site 6 out
of 8 in the The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K984
b:17.2
occ:1.00
|
OG
|
D:SER22
|
2.5
|
17.3
|
1.0
|
OD2
|
C:ASP264
|
2.5
|
20.3
|
1.0
|
O
|
D:GLY20
|
2.6
|
17.6
|
1.0
|
O
|
D:ASN460
|
2.6
|
17.1
|
1.0
|
O
|
C:PHE266
|
2.8
|
12.7
|
1.0
|
OD1
|
C:ASP264
|
3.1
|
17.6
|
1.0
|
CG
|
C:ASP264
|
3.2
|
18.9
|
1.0
|
CB
|
D:SER22
|
3.5
|
19.2
|
1.0
|
C
|
D:ASN460
|
3.6
|
18.4
|
1.0
|
N
|
D:SER22
|
3.7
|
17.9
|
1.0
|
O
|
C:HOH1052
|
3.7
|
25.4
|
1.0
|
C
|
C:PHE266
|
3.8
|
16.6
|
1.0
|
C
|
D:GLY20
|
3.8
|
17.4
|
1.0
|
CB
|
C:PHE266
|
3.9
|
13.4
|
1.0
|
CA
|
D:ASN460
|
3.9
|
18.4
|
1.0
|
CB
|
D:PRO19
|
4.0
|
16.4
|
1.0
|
CA
|
D:SER22
|
4.1
|
19.4
|
1.0
|
C
|
D:LEU21
|
4.2
|
16.8
|
1.0
|
N
|
D:GLY20
|
4.3
|
17.2
|
1.0
|
CA
|
C:PHE266
|
4.3
|
15.1
|
1.0
|
CA
|
D:LEU21
|
4.5
|
16.8
|
1.0
|
N
|
C:PHE266
|
4.6
|
15.8
|
1.0
|
N
|
D:LEU21
|
4.6
|
17.3
|
1.0
|
CB
|
D:ASN460
|
4.6
|
19.3
|
1.0
|
O
|
D:CYS459
|
4.6
|
18.1
|
1.0
|
CB
|
C:ASP264
|
4.6
|
16.4
|
1.0
|
CG
|
C:PHE266
|
4.7
|
15.6
|
1.0
|
C
|
D:PRO19
|
4.7
|
16.5
|
1.0
|
CA
|
D:PRO19
|
4.8
|
16.2
|
1.0
|
CA
|
D:GLY20
|
4.8
|
17.7
|
1.0
|
N
|
D:CYS461
|
4.8
|
16.1
|
1.0
|
N
|
C:SER267
|
4.9
|
15.8
|
1.0
|
ND2
|
D:ASN460
|
4.9
|
21.6
|
1.0
|
O
|
C:HOH1023
|
4.9
|
15.9
|
1.0
|
O
|
D:LEU21
|
5.0
|
16.3
|
1.0
|
|
Potassium binding site 7 out
of 8 in 1pvn
Go back to
Potassium Binding Sites List in 1pvn
Potassium binding site 7 out
of 8 in the The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K985
b:17.9
occ:1.00
|
O
|
C:GLU485
|
2.6
|
16.0
|
1.0
|
O
|
B:GLY316
|
2.6
|
14.4
|
1.0
|
O
|
B:GLY314
|
2.6
|
20.3
|
1.0
|
O
|
B:CYS319
|
2.7
|
15.9
|
1.0
|
O
|
C:GLY487
|
2.9
|
19.2
|
1.0
|
O
|
C:GLY486
|
3.1
|
19.4
|
1.0
|
C
|
C:GLY486
|
3.3
|
18.7
|
1.0
|
C
|
C:GLY487
|
3.6
|
19.6
|
1.0
|
O
|
C:HOH1029
|
3.6
|
20.8
|
1.0
|
C
|
B:CYS319
|
3.7
|
16.8
|
1.0
|
C
|
C:GLU485
|
3.7
|
16.7
|
1.0
|
C
|
B:GLY316
|
3.7
|
17.3
|
1.0
|
C
|
B:GLY314
|
3.7
|
17.4
|
1.0
|
CA
|
C:GLY486
|
3.8
|
17.1
|
1.0
|
N
|
C:GLY487
|
3.8
|
18.9
|
1.0
|
C
|
B:GLY315
|
3.9
|
17.9
|
1.0
|
CB
|
B:CYS319
|
3.9
|
16.6
|
1.0
|
N
|
B:GLY316
|
4.0
|
17.4
|
1.0
|
CD2
|
C:HIS489
|
4.0
|
15.3
|
1.0
|
O
|
B:GLY315
|
4.0
|
17.4
|
1.0
|
CA
|
B:CYS319
|
4.1
|
16.6
|
1.0
|
N
|
B:CYS319
|
4.2
|
15.6
|
1.0
|
CA
|
C:GLY487
|
4.2
|
18.8
|
1.0
|
N
|
C:GLY486
|
4.2
|
16.2
|
1.0
|
CA
|
B:GLY315
|
4.2
|
17.6
|
1.0
|
NE2
|
C:HIS489
|
4.3
|
16.5
|
1.0
|
CA
|
B:GLY316
|
4.4
|
16.0
|
1.0
|
N
|
B:GLY315
|
4.4
|
18.3
|
1.0
|
N
|
C:ALA488
|
4.5
|
19.8
|
1.0
|
SG
|
B:CYS319
|
4.7
|
18.9
|
1.0
|
N
|
B:SER317
|
4.7
|
15.3
|
1.0
|
CA
|
B:GLY314
|
4.8
|
18.6
|
1.0
|
N
|
B:ILE320
|
4.8
|
16.2
|
1.0
|
CA
|
C:ALA488
|
4.8
|
19.3
|
1.0
|
C
|
B:SER317
|
4.9
|
16.8
|
1.0
|
O
|
B:SER317
|
4.9
|
18.3
|
1.0
|
CA
|
C:GLU485
|
4.9
|
17.0
|
1.0
|
CA
|
B:SER317
|
4.9
|
17.8
|
1.0
|
|
Potassium binding site 8 out
of 8 in 1pvn
Go back to
Potassium Binding Sites List in 1pvn
Potassium binding site 8 out
of 8 in the The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of The Crystal Structure of the Complex Between Imp Dehydrogenase Catalytic Domain and A Transition State Analogue Mzp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K983
b:14.1
occ:1.00
|
O
|
C:GLY316
|
2.6
|
12.5
|
1.0
|
O
|
D:GLU485
|
2.6
|
17.6
|
1.0
|
O
|
C:CYS319
|
2.7
|
12.3
|
1.0
|
O
|
D:GLY487
|
2.7
|
19.9
|
1.0
|
O
|
C:GLY314
|
2.7
|
17.4
|
1.0
|
O
|
D:GLY486
|
3.1
|
19.7
|
1.0
|
C
|
D:GLY486
|
3.3
|
19.4
|
1.0
|
C
|
D:GLY487
|
3.4
|
18.9
|
1.0
|
C
|
C:CYS319
|
3.6
|
14.1
|
1.0
|
C
|
C:GLY316
|
3.7
|
14.4
|
1.0
|
N
|
D:GLY487
|
3.7
|
19.8
|
1.0
|
O
|
D:HOH1009
|
3.7
|
18.8
|
1.0
|
C
|
D:GLU485
|
3.7
|
18.2
|
1.0
|
C
|
C:GLY314
|
3.8
|
17.3
|
1.0
|
C
|
C:GLY315
|
3.9
|
15.7
|
1.0
|
CA
|
D:GLY486
|
3.9
|
18.7
|
1.0
|
CB
|
C:CYS319
|
3.9
|
14.1
|
1.0
|
CD2
|
D:HIS489
|
4.0
|
17.0
|
1.0
|
CA
|
D:GLY487
|
4.0
|
19.9
|
1.0
|
N
|
C:GLY316
|
4.0
|
14.4
|
1.0
|
O
|
C:GLY315
|
4.0
|
14.6
|
1.0
|
CA
|
C:CYS319
|
4.1
|
13.2
|
1.0
|
N
|
C:CYS319
|
4.1
|
14.2
|
1.0
|
N
|
D:ALA488
|
4.2
|
18.0
|
1.0
|
N
|
D:GLY486
|
4.3
|
17.6
|
1.0
|
CA
|
C:GLY315
|
4.3
|
15.0
|
1.0
|
NE2
|
D:HIS489
|
4.3
|
17.4
|
1.0
|
CA
|
C:GLY316
|
4.4
|
13.6
|
1.0
|
N
|
C:GLY315
|
4.5
|
16.1
|
1.0
|
CA
|
D:ALA488
|
4.5
|
18.0
|
1.0
|
SG
|
C:CYS319
|
4.6
|
19.1
|
1.0
|
N
|
C:SER317
|
4.7
|
14.8
|
1.0
|
N
|
C:ILE320
|
4.8
|
14.3
|
1.0
|
C
|
C:SER317
|
4.8
|
16.3
|
1.0
|
O
|
C:SER317
|
4.8
|
16.9
|
1.0
|
CA
|
C:GLY314
|
4.8
|
17.4
|
1.0
|
CA
|
C:SER317
|
4.9
|
15.2
|
1.0
|
CA
|
D:GLU485
|
5.0
|
17.4
|
1.0
|
O
|
D:HOH1220
|
5.0
|
45.4
|
1.0
|
|
Reference:
L.Gan,
M.Seyedsayamdost,
S.Shuto,
A.Matsuda,
G.A.Petsko,
L.Hedstrom.
The Immunosuppressive Agent Mizoribine Monophosphate Forms A Transition State Analogue Complex with Inosine Monophosphate Dehydrogenase Biochemistry V. 42 857 2003.
ISSN: ISSN 0006-2960
PubMed: 12549902
DOI: 10.1021/BI0271401
Page generated: Mon Aug 12 05:13:43 2024
|