Cobalt in PDB 2qb7: Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex
Enzymatic activity of Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex
All present enzymatic activity of Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex:
3.6.1.11;
Protein crystallography data
The structure of Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex, PDB code: 2qb7
was solved by
S.A.White,
E.Ugochukwu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
67.42 /
1.60
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
79.992,
83.039,
118.900,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.1 /
20.1
|
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex
(pdb code 2qb7). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the
Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex, PDB code: 2qb7:
Jump to Cobalt binding site number:
1;
2;
3;
4;
Cobalt binding site 1 out
of 4 in 2qb7
Go back to
Cobalt Binding Sites List in 2qb7
Cobalt binding site 1 out
of 4 in the Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 1 of Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Co401
b:10.6
occ:1.00
|
O2
|
A:PO4501
|
2.0
|
13.3
|
1.0
|
OD2
|
A:ASP41
|
2.1
|
10.5
|
1.0
|
OD1
|
A:ASP127
|
2.1
|
9.3
|
1.0
|
NE2
|
A:HIS148
|
2.2
|
11.8
|
1.0
|
O
|
A:HOH1354
|
2.2
|
15.0
|
1.0
|
CG
|
A:ASP127
|
2.9
|
10.3
|
1.0
|
OD2
|
A:ASP127
|
3.0
|
10.5
|
1.0
|
CE1
|
A:HIS148
|
3.1
|
10.8
|
1.0
|
CG
|
A:ASP41
|
3.1
|
10.0
|
1.0
|
CD2
|
A:HIS148
|
3.3
|
9.3
|
1.0
|
P
|
A:PO4501
|
3.3
|
14.1
|
1.0
|
CB
|
A:ASP41
|
3.5
|
9.2
|
1.0
|
O1
|
A:PO4501
|
3.7
|
14.9
|
1.0
|
O
|
A:HOH1293
|
3.9
|
21.9
|
1.0
|
CE1
|
A:HIS149
|
3.9
|
10.8
|
1.0
|
O3
|
A:PO4501
|
4.1
|
15.0
|
1.0
|
CB
|
A:CYS169
|
4.2
|
11.2
|
1.0
|
N
|
A:CYS169
|
4.2
|
11.5
|
1.0
|
OD1
|
A:ASP41
|
4.2
|
10.7
|
1.0
|
ND1
|
A:HIS148
|
4.2
|
10.2
|
1.0
|
O
|
A:HOH1292
|
4.3
|
18.2
|
1.0
|
CB
|
A:ASP127
|
4.3
|
9.7
|
1.0
|
O4
|
A:PO4501
|
4.3
|
16.3
|
1.0
|
CG
|
A:HIS148
|
4.4
|
9.6
|
1.0
|
NE2
|
A:HIS149
|
4.4
|
11.1
|
1.0
|
OD2
|
A:ASP202
|
4.4
|
14.3
|
1.0
|
OD2
|
A:ASP39
|
4.7
|
12.2
|
1.0
|
CA
|
A:CYS169
|
4.8
|
11.6
|
1.0
|
CA
|
A:ASP127
|
4.9
|
10.7
|
1.0
|
ND1
|
A:HIS149
|
4.9
|
10.8
|
1.0
|
CA
|
A:ASP41
|
4.9
|
9.7
|
1.0
|
|
Cobalt binding site 2 out
of 4 in 2qb7
Go back to
Cobalt Binding Sites List in 2qb7
Cobalt binding site 2 out
of 4 in the Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 2 of Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Co402
b:11.8
occ:1.00
|
O2
|
A:PO4503
|
2.0
|
12.8
|
1.0
|
O3
|
A:PO4501
|
2.1
|
15.0
|
1.0
|
O
|
A:HOH1309
|
2.2
|
11.5
|
1.0
|
O
|
A:HOH1355
|
2.2
|
13.6
|
1.0
|
O
|
A:HOH1010
|
2.2
|
11.3
|
1.0
|
O
|
A:HOH979
|
2.2
|
11.2
|
1.0
|
P
|
A:PO4501
|
3.3
|
14.1
|
1.0
|
P
|
A:PO4503
|
3.3
|
13.7
|
1.0
|
O4
|
A:PO4503
|
3.7
|
14.3
|
1.0
|
O1
|
A:PO4501
|
3.8
|
14.9
|
1.0
|
OD2
|
A:ASP39
|
3.8
|
12.2
|
1.0
|
O4
|
A:PO4501
|
3.8
|
16.3
|
1.0
|
O
|
A:HOH1292
|
3.9
|
18.2
|
1.0
|
NH2
|
A:ARG381
|
4.0
|
11.9
|
1.0
|
O3
|
A:PO4503
|
4.1
|
14.4
|
1.0
|
O
|
A:HOH929
|
4.1
|
13.6
|
1.0
|
O4
|
A:PO4502
|
4.1
|
21.8
|
1.0
|
O1
|
A:PO4502
|
4.1
|
17.8
|
1.0
|
O
|
A:HOH917
|
4.2
|
12.4
|
1.0
|
OD2
|
A:ASP266
|
4.3
|
11.8
|
1.0
|
O
|
A:HOH1140
|
4.3
|
22.0
|
1.0
|
O
|
A:HOH1017
|
4.3
|
14.8
|
1.0
|
OD1
|
A:ASP266
|
4.4
|
10.8
|
1.0
|
O1
|
A:PO4503
|
4.5
|
13.1
|
1.0
|
O2
|
A:PO4501
|
4.6
|
13.3
|
1.0
|
P
|
A:PO4502
|
4.7
|
19.8
|
1.0
|
CG
|
A:ASP266
|
4.8
|
9.4
|
1.0
|
CG
|
A:ASP39
|
4.8
|
12.3
|
1.0
|
OG
|
A:SER37
|
4.9
|
13.0
|
1.0
|
|
Cobalt binding site 3 out
of 4 in 2qb7
Go back to
Cobalt Binding Sites List in 2qb7
Cobalt binding site 3 out
of 4 in the Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 3 of Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co401
b:14.6
occ:1.00
|
OD2
|
B:ASP41
|
2.1
|
13.5
|
1.0
|
OD1
|
B:ASP127
|
2.1
|
13.1
|
1.0
|
O2
|
B:PO4501
|
2.1
|
19.9
|
1.0
|
NE2
|
B:HIS148
|
2.2
|
15.5
|
1.0
|
O
|
B:HOH1219
|
2.2
|
16.1
|
1.0
|
CG
|
B:ASP127
|
2.9
|
13.0
|
1.0
|
CE1
|
B:HIS148
|
3.0
|
14.8
|
1.0
|
OD2
|
B:ASP127
|
3.0
|
13.1
|
1.0
|
CG
|
B:ASP41
|
3.1
|
14.0
|
1.0
|
CD2
|
B:HIS148
|
3.3
|
15.7
|
1.0
|
P
|
B:PO4501
|
3.4
|
21.4
|
1.0
|
CB
|
B:ASP41
|
3.6
|
13.6
|
1.0
|
O3
|
B:PO4501
|
3.8
|
20.8
|
1.0
|
CE1
|
B:HIS149
|
3.9
|
17.3
|
1.0
|
O
|
B:HOH1163
|
3.9
|
26.6
|
1.0
|
ND1
|
B:HIS148
|
4.2
|
14.7
|
1.0
|
CB
|
B:CYS169
|
4.2
|
14.1
|
1.0
|
OD1
|
B:ASP41
|
4.2
|
15.0
|
1.0
|
N
|
B:CYS169
|
4.2
|
13.9
|
1.0
|
O4
|
B:PO4501
|
4.2
|
17.7
|
1.0
|
O
|
B:HOH1161
|
4.3
|
23.5
|
1.0
|
CB
|
B:ASP127
|
4.3
|
13.5
|
1.0
|
CG
|
B:HIS148
|
4.3
|
15.5
|
1.0
|
OD2
|
B:ASP202
|
4.4
|
15.7
|
1.0
|
O1
|
B:PO4501
|
4.4
|
20.8
|
1.0
|
NE2
|
B:HIS149
|
4.4
|
17.6
|
1.0
|
OD2
|
B:ASP39
|
4.7
|
17.6
|
1.0
|
CA
|
B:ASP127
|
4.9
|
14.0
|
1.0
|
ND1
|
B:HIS149
|
4.9
|
16.2
|
1.0
|
CA
|
B:CYS169
|
4.9
|
14.1
|
1.0
|
CA
|
B:ASP41
|
5.0
|
13.6
|
1.0
|
|
Cobalt binding site 4 out
of 4 in 2qb7
Go back to
Cobalt Binding Sites List in 2qb7
Cobalt binding site 4 out
of 4 in the Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 4 of Saccharomyces Cerevisiae Cytosolic Exopolyphosphatase, Phosphate Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co402
b:19.1
occ:1.00
|
O2
|
B:PO4502
|
2.1
|
19.8
|
1.0
|
O4
|
B:PO4501
|
2.1
|
17.7
|
1.0
|
O
|
B:HOH1220
|
2.2
|
22.4
|
1.0
|
O
|
B:HOH1183
|
2.2
|
17.5
|
1.0
|
O
|
B:HOH953
|
2.2
|
14.2
|
1.0
|
O
|
B:HOH973
|
2.3
|
19.2
|
1.0
|
P
|
B:PO4501
|
3.3
|
21.4
|
1.0
|
P
|
B:PO4502
|
3.4
|
19.7
|
1.0
|
O3
|
B:PO4502
|
3.8
|
20.3
|
1.0
|
O3
|
B:PO4501
|
3.8
|
20.8
|
1.0
|
O1
|
B:PO4501
|
3.8
|
20.8
|
1.0
|
OD2
|
B:ASP39
|
3.9
|
17.6
|
1.0
|
O
|
B:HOH1161
|
3.9
|
23.5
|
1.0
|
O4
|
B:PO4503
|
4.1
|
28.3
|
1.0
|
O1
|
B:PO4502
|
4.1
|
19.4
|
1.0
|
O
|
B:HOH962
|
4.1
|
21.0
|
1.0
|
O1
|
B:PO4503
|
4.1
|
28.9
|
1.0
|
NH2
|
B:ARG381
|
4.1
|
19.0
|
1.0
|
O
|
B:HOH919
|
4.1
|
18.6
|
1.0
|
OD2
|
B:ASP266
|
4.3
|
19.3
|
1.0
|
O
|
B:HOH1188
|
4.3
|
40.8
|
1.0
|
OD1
|
B:ASP266
|
4.4
|
17.0
|
1.0
|
O
|
B:HOH1081
|
4.4
|
19.4
|
1.0
|
O4
|
B:PO4502
|
4.5
|
19.4
|
1.0
|
O2
|
B:PO4501
|
4.5
|
19.9
|
1.0
|
P
|
B:PO4503
|
4.7
|
28.5
|
1.0
|
CG
|
B:ASP266
|
4.8
|
18.3
|
1.0
|
CG
|
B:ASP39
|
4.8
|
17.1
|
1.0
|
OG
|
B:SER37
|
5.0
|
18.2
|
1.0
|
|
Reference:
E.Ugochukwu,
A.L.Lovering,
O.C.Mather,
T.W.Young,
S.A.White.
The Crystal Structure of the Cytosolic Exopolyphosphatase From Saccharomyces Cerevisiae Reveals the Basis For Substrate Specificity. J.Mol.Biol. V. 371 1007 2007.
ISSN: ISSN 0022-2836
PubMed: 17599355
DOI: 10.1016/J.JMB.2007.05.066
Page generated: Tue Jul 30 15:28:57 2024
|