Potassium in PDB 7t7k: Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+
Protein crystallography data
The structure of Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+, PDB code: 7t7k
was solved by
A.Jacewicz,
A.M.Sanchez,
S.Shuman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.42 /
1.90
|
Space group
|
P 2 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
58.654,
116.314,
151.862,
90,
90,
90
|
R / Rfree (%)
|
16.4 /
19.6
|
Other elements in 7t7k:
The structure of Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+ also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+
(pdb code 7t7k). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the
Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+, PDB code: 7t7k:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 7t7k
Go back to
Potassium Binding Sites List in 7t7k
Potassium binding site 1 out
of 4 in the Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K501
b:23.8
occ:0.47
|
OG1
|
B:THR333
|
2.6
|
19.3
|
1.0
|
O
|
B:HOH872
|
2.7
|
34.5
|
1.0
|
O
|
B:PRO330
|
2.8
|
22.1
|
1.0
|
OD2
|
B:ASP88
|
2.8
|
34.9
|
1.0
|
CG
|
B:ASP88
|
3.4
|
35.0
|
1.0
|
O
|
B:THR333
|
3.6
|
21.0
|
1.0
|
CB
|
B:THR333
|
3.6
|
21.5
|
1.0
|
C
|
B:PRO330
|
3.6
|
21.2
|
1.0
|
C
|
B:THR333
|
3.6
|
21.2
|
1.0
|
CA
|
B:PRO330
|
3.7
|
21.8
|
1.0
|
CB
|
B:PRO330
|
3.8
|
23.7
|
1.0
|
CB
|
B:ASP88
|
3.9
|
27.8
|
1.0
|
CA
|
B:THR333
|
4.0
|
21.6
|
1.0
|
CE2
|
B:PHE280
|
4.0
|
26.8
|
1.0
|
CZ
|
B:PHE280
|
4.2
|
28.1
|
1.0
|
N
|
B:THR334
|
4.2
|
17.7
|
1.0
|
OD1
|
B:ASP88
|
4.2
|
29.1
|
1.0
|
N
|
B:THR333
|
4.2
|
15.5
|
1.0
|
CG2
|
B:THR334
|
4.3
|
17.8
|
1.0
|
NE
|
B:ARG118
|
4.3
|
20.9
|
1.0
|
NH2
|
B:ARG118
|
4.7
|
24.2
|
1.0
|
OD2
|
B:ASP279
|
4.8
|
37.4
|
1.0
|
O
|
B:HOH693
|
4.8
|
20.4
|
1.0
|
CZ
|
B:ARG118
|
4.8
|
21.9
|
1.0
|
CA
|
B:THR334
|
4.8
|
17.5
|
1.0
|
N
|
B:PHE331
|
4.9
|
19.7
|
1.0
|
CG2
|
B:THR333
|
4.9
|
19.4
|
1.0
|
|
Potassium binding site 2 out
of 4 in 7t7k
Go back to
Potassium Binding Sites List in 7t7k
Potassium binding site 2 out
of 4 in the Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K501
b:61.0
occ:0.90
|
O
|
A:HOH860
|
2.7
|
41.5
|
1.0
|
O
|
A:HOH964
|
2.8
|
38.8
|
1.0
|
O
|
A:ASN75
|
2.9
|
23.5
|
1.0
|
O
|
A:HOH796
|
3.0
|
47.7
|
1.0
|
O
|
A:HOH953
|
3.7
|
50.2
|
1.0
|
O4
|
A:PO4506
|
3.8
|
61.1
|
1.0
|
C
|
A:ASN75
|
4.0
|
26.4
|
1.0
|
O
|
A:HOH744
|
4.3
|
31.1
|
1.0
|
CA
|
A:ASN75
|
4.6
|
25.8
|
1.0
|
O
|
A:HOH887
|
4.6
|
46.7
|
1.0
|
CB
|
A:ASN75
|
4.6
|
27.1
|
1.0
|
O
|
A:ASP76
|
4.8
|
24.8
|
1.0
|
CB
|
A:ASP76
|
4.8
|
23.4
|
1.0
|
OD1
|
A:ASN75
|
4.9
|
36.5
|
1.0
|
|
Potassium binding site 3 out
of 4 in 7t7k
Go back to
Potassium Binding Sites List in 7t7k
Potassium binding site 3 out
of 4 in the Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K502
b:48.8
occ:0.69
|
O
|
A:HOH863
|
2.5
|
40.8
|
1.0
|
OE1
|
A:GLN211
|
2.9
|
29.6
|
1.0
|
OE1
|
A:GLN208
|
2.9
|
56.9
|
1.0
|
O
|
A:HOH725
|
3.3
|
48.3
|
1.0
|
CB
|
A:GLN211
|
3.6
|
27.1
|
1.0
|
CD
|
A:GLN211
|
3.9
|
29.2
|
1.0
|
CB
|
A:ALA150
|
3.9
|
31.3
|
1.0
|
CA
|
A:SER147
|
4.0
|
24.6
|
1.0
|
CD
|
A:GLN208
|
4.0
|
58.2
|
1.0
|
OG
|
A:SER147
|
4.2
|
33.7
|
1.0
|
CB
|
A:SER147
|
4.2
|
32.5
|
1.0
|
O
|
A:GLN208
|
4.3
|
33.8
|
1.0
|
CG
|
A:GLN211
|
4.3
|
24.9
|
1.0
|
O
|
A:GLN211
|
4.4
|
34.5
|
1.0
|
CB
|
A:GLN208
|
4.5
|
45.9
|
1.0
|
N
|
A:ALA150
|
4.6
|
33.3
|
1.0
|
O
|
A:SER147
|
4.6
|
26.9
|
1.0
|
CG
|
A:GLN208
|
4.6
|
53.0
|
1.0
|
C
|
A:SER147
|
4.6
|
30.0
|
1.0
|
O
|
A:HOH724
|
4.7
|
31.5
|
1.0
|
C
|
A:GLN211
|
4.8
|
35.8
|
1.0
|
CA
|
A:GLN211
|
4.8
|
28.4
|
1.0
|
O
|
A:SER146
|
4.8
|
34.1
|
1.0
|
CA
|
A:ALA150
|
4.9
|
36.5
|
1.0
|
NE2
|
A:GLN211
|
5.0
|
24.2
|
1.0
|
|
Potassium binding site 4 out
of 4 in 7t7k
Go back to
Potassium Binding Sites List in 7t7k
Potassium binding site 4 out
of 4 in the Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Structure of SPAC806.04C Protein From Fission Yeast Bound to CO2+ within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K503
b:46.0
occ:0.42
|
OE1
|
B:GLU206
|
2.6
|
33.4
|
1.0
|
O
|
A:HOH906
|
2.6
|
46.1
|
1.0
|
OE1
|
A:GLU414
|
2.9
|
34.5
|
1.0
|
CD
|
A:GLU414
|
2.9
|
53.7
|
1.0
|
O
|
B:HOH662
|
3.1
|
33.2
|
1.0
|
OE2
|
B:GLU206
|
3.2
|
38.0
|
1.0
|
CD
|
B:GLU206
|
3.2
|
43.1
|
1.0
|
CG
|
A:GLU414
|
3.4
|
38.3
|
1.0
|
OE2
|
A:GLU414
|
3.4
|
60.3
|
1.0
|
CB
|
A:GLU414
|
3.6
|
33.7
|
1.0
|
CA
|
A:GLY411
|
4.2
|
25.4
|
1.0
|
O
|
B:HOH635
|
4.4
|
21.6
|
1.0
|
O
|
B:HOH668
|
4.5
|
47.0
|
1.0
|
O
|
A:HOH865
|
4.6
|
30.5
|
1.0
|
CG
|
B:GLU206
|
4.6
|
27.6
|
1.0
|
O
|
A:GLY411
|
4.8
|
24.6
|
1.0
|
N
|
A:GLY411
|
4.9
|
22.7
|
1.0
|
C
|
A:GLY411
|
5.0
|
25.4
|
1.0
|
CA
|
A:GLU414
|
5.0
|
27.8
|
1.0
|
|
Reference:
A.M.Sanchez,
A.Jacewicz,
S.Shuman.
Fission Yeast DUF89 and DUF8901 Are Cobalt/Nickel-Dependent Phosphatase-Pyrophosphatases That Act Via A Covalent Aspartyl-Phosphate Intermediate. J.Biol.Chem. V. 298 01851 2022.
ISSN: ESSN 1083-351X
PubMed: 35314193
DOI: 10.1016/J.JBC.2022.101851
Page generated: Mon Aug 12 21:14:06 2024
|