Cobalt in PDB 3ur2: Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V
Enzymatic activity of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V
All present enzymatic activity of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V:
3.1.8.1;
Protein crystallography data
The structure of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V, PDB code: 3ur2
was solved by
P.Tsai,
N.G.Fox,
Y.Li,
D.P.Barondeau,
F.M.Raushel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.00
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
85.061,
85.243,
87.667,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.6 /
24.6
|
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V
(pdb code 3ur2). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the
Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V, PDB code: 3ur2:
Jump to Cobalt binding site number:
1;
2;
3;
4;
Cobalt binding site 1 out
of 4 in 3ur2
Go back to
Cobalt Binding Sites List in 3ur2
Cobalt binding site 1 out
of 4 in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 1 of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Co801
b:27.1
occ:1.00
|
NE2
|
A:HIS230
|
2.0
|
19.7
|
1.0
|
O
|
A:HOH1190
|
2.0
|
28.9
|
1.0
|
O
|
A:HOH1244
|
2.1
|
27.4
|
1.0
|
ND1
|
A:HIS201
|
2.1
|
24.8
|
1.0
|
OQ2
|
A:KCX169
|
2.2
|
21.4
|
1.0
|
O
|
A:HOH1189
|
2.5
|
30.8
|
1.0
|
CD2
|
A:HIS230
|
2.9
|
20.2
|
1.0
|
CE1
|
A:HIS201
|
3.0
|
26.2
|
1.0
|
CE1
|
A:HIS230
|
3.1
|
20.8
|
1.0
|
CG
|
A:HIS201
|
3.2
|
25.8
|
1.0
|
CX
|
A:KCX169
|
3.2
|
24.8
|
1.0
|
OQ1
|
A:KCX169
|
3.6
|
24.6
|
1.0
|
CB
|
A:HIS201
|
3.6
|
24.8
|
1.0
|
CO
|
A:CO802
|
3.8
|
23.7
|
1.0
|
O
|
A:HOH1151
|
3.8
|
46.3
|
1.0
|
NE1
|
A:TRP131
|
4.0
|
22.2
|
1.0
|
CG
|
A:HIS230
|
4.1
|
19.0
|
1.0
|
ND1
|
A:HIS230
|
4.1
|
20.7
|
1.0
|
NE2
|
A:HIS201
|
4.2
|
24.0
|
1.0
|
OD2
|
A:ASP301
|
4.2
|
23.6
|
1.0
|
CD2
|
A:HIS201
|
4.3
|
25.1
|
1.0
|
O
|
A:HOH1350
|
4.3
|
50.9
|
1.0
|
NE2
|
A:HIS55
|
4.3
|
21.0
|
1.0
|
NZ
|
A:KCX169
|
4.4
|
23.4
|
1.0
|
O
|
A:HOH1349
|
4.4
|
45.0
|
1.0
|
CA
|
A:HIS201
|
4.5
|
25.3
|
1.0
|
CE1
|
A:HIS55
|
4.5
|
18.7
|
1.0
|
CD1
|
A:TRP131
|
4.8
|
22.1
|
1.0
|
CE
|
A:KCX169
|
4.8
|
21.0
|
1.0
|
|
Cobalt binding site 2 out
of 4 in 3ur2
Go back to
Cobalt Binding Sites List in 3ur2
Cobalt binding site 2 out
of 4 in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 2 of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Co802
b:23.7
occ:1.00
|
NE2
|
A:HIS57
|
2.0
|
22.8
|
1.0
|
O
|
A:HOH1244
|
2.0
|
27.4
|
1.0
|
NE2
|
A:HIS55
|
2.3
|
21.0
|
1.0
|
OD1
|
A:ASP301
|
2.3
|
23.4
|
1.0
|
OQ1
|
A:KCX169
|
2.3
|
24.6
|
1.0
|
CE1
|
A:HIS57
|
2.9
|
24.4
|
1.0
|
CD2
|
A:HIS55
|
3.0
|
20.4
|
1.0
|
CD2
|
A:HIS57
|
3.1
|
23.6
|
1.0
|
CG
|
A:ASP301
|
3.1
|
22.7
|
1.0
|
CX
|
A:KCX169
|
3.1
|
24.8
|
1.0
|
O
|
A:HOH1350
|
3.2
|
50.9
|
1.0
|
OD2
|
A:ASP301
|
3.3
|
23.6
|
1.0
|
CE1
|
A:HIS55
|
3.4
|
18.7
|
1.0
|
OQ2
|
A:KCX169
|
3.5
|
21.4
|
1.0
|
O
|
A:HOH1349
|
3.7
|
45.0
|
1.0
|
CO
|
A:CO801
|
3.8
|
27.1
|
1.0
|
ND1
|
A:HIS57
|
4.1
|
21.0
|
1.0
|
NZ
|
A:KCX169
|
4.1
|
23.4
|
1.0
|
CG2
|
A:VAL101
|
4.2
|
18.0
|
1.0
|
CG
|
A:HIS57
|
4.2
|
23.0
|
1.0
|
CE1
|
A:HIS230
|
4.2
|
20.8
|
1.0
|
CG
|
A:HIS55
|
4.2
|
19.7
|
1.0
|
O
|
A:HOH1190
|
4.3
|
28.9
|
1.0
|
NE2
|
A:HIS230
|
4.4
|
19.7
|
1.0
|
ND1
|
A:HIS55
|
4.4
|
21.4
|
1.0
|
CB
|
A:ASP301
|
4.4
|
23.3
|
1.0
|
CA
|
A:ASP301
|
4.9
|
22.0
|
1.0
|
O
|
A:HOH1189
|
4.9
|
30.8
|
1.0
|
O
|
A:HOH1255
|
4.9
|
41.9
|
1.0
|
|
Cobalt binding site 3 out
of 4 in 3ur2
Go back to
Cobalt Binding Sites List in 3ur2
Cobalt binding site 3 out
of 4 in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 3 of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co803
b:39.4
occ:1.00
|
NE2
|
B:HIS57
|
2.0
|
37.3
|
1.0
|
OQ2
|
B:KCX169
|
2.2
|
37.1
|
1.0
|
OD1
|
B:ASP301
|
2.2
|
36.6
|
1.0
|
NE2
|
B:HIS55
|
2.4
|
37.4
|
1.0
|
O
|
B:HOH1245
|
2.5
|
40.3
|
1.0
|
CE1
|
B:HIS57
|
3.0
|
36.0
|
1.0
|
CD2
|
B:HIS57
|
3.0
|
34.8
|
1.0
|
CD2
|
B:HIS55
|
3.0
|
37.0
|
1.0
|
CX
|
B:KCX169
|
3.0
|
38.9
|
1.0
|
CG
|
B:ASP301
|
3.1
|
36.2
|
1.0
|
OD2
|
B:ASP301
|
3.3
|
36.3
|
1.0
|
OQ1
|
B:KCX169
|
3.4
|
41.7
|
1.0
|
CE1
|
B:HIS55
|
3.6
|
36.1
|
1.0
|
O
|
B:HOH1375
|
3.7
|
68.4
|
1.0
|
CO
|
B:CO804
|
3.9
|
49.0
|
1.0
|
NZ
|
B:KCX169
|
4.1
|
40.4
|
1.0
|
ND1
|
B:HIS57
|
4.1
|
35.3
|
1.0
|
CG
|
B:HIS57
|
4.1
|
35.3
|
1.0
|
CG2
|
B:VAL101
|
4.1
|
32.6
|
1.0
|
CG
|
B:HIS55
|
4.3
|
38.0
|
1.0
|
O
|
B:HOH1300
|
4.4
|
63.7
|
1.0
|
CB
|
B:ASP301
|
4.4
|
37.7
|
1.0
|
CE1
|
B:HIS230
|
4.4
|
49.5
|
1.0
|
ND1
|
B:HIS55
|
4.5
|
37.2
|
1.0
|
NE2
|
B:HIS230
|
4.7
|
50.7
|
1.0
|
CA
|
B:ASP301
|
4.9
|
39.4
|
1.0
|
|
Cobalt binding site 4 out
of 4 in 3ur2
Go back to
Cobalt Binding Sites List in 3ur2
Cobalt binding site 4 out
of 4 in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V
Mono view
Stereo pair view
|
A full contact list of Cobalt with other atoms in the Co binding
site number 4 of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Co804
b:49.0
occ:1.00
|
ND1
|
B:HIS201
|
1.7
|
48.3
|
1.0
|
OQ1
|
B:KCX169
|
2.1
|
41.7
|
1.0
|
O
|
B:HOH1245
|
2.1
|
40.3
|
1.0
|
NE2
|
B:HIS230
|
2.3
|
50.7
|
1.0
|
CE1
|
B:HIS201
|
2.4
|
48.6
|
1.0
|
CE1
|
B:HIS230
|
2.9
|
49.5
|
1.0
|
CG
|
B:HIS201
|
3.0
|
47.6
|
1.0
|
CX
|
B:KCX169
|
3.2
|
38.9
|
1.0
|
CD2
|
B:HIS230
|
3.4
|
50.0
|
1.0
|
OQ2
|
B:KCX169
|
3.6
|
37.1
|
1.0
|
NE2
|
B:HIS201
|
3.6
|
47.6
|
1.0
|
CB
|
B:HIS201
|
3.6
|
46.5
|
1.0
|
CO
|
B:CO803
|
3.9
|
39.4
|
1.0
|
CD2
|
B:HIS201
|
3.9
|
47.6
|
1.0
|
NE1
|
B:TRP131
|
3.9
|
42.8
|
1.0
|
ND1
|
B:HIS230
|
3.9
|
51.0
|
1.0
|
CG
|
B:HIS230
|
4.2
|
49.6
|
1.0
|
NE2
|
B:HIS55
|
4.3
|
37.4
|
1.0
|
NZ
|
B:KCX169
|
4.3
|
40.4
|
1.0
|
OD2
|
B:ASP301
|
4.3
|
36.3
|
1.0
|
CA
|
B:HIS201
|
4.5
|
46.1
|
1.0
|
CE1
|
B:HIS55
|
4.6
|
36.1
|
1.0
|
CE
|
B:KCX169
|
4.7
|
39.2
|
1.0
|
CD1
|
B:TRP131
|
4.7
|
42.4
|
1.0
|
CE2
|
B:TRP131
|
4.9
|
42.3
|
1.0
|
|
Reference:
P.C.Tsai,
N.Fox,
A.N.Bigley,
S.P.Harvey,
D.P.Barondeau,
F.M.Raushel.
Enzymes For the Homeland Defense: Optimizing Phosphotriesterase For the Hydrolysis of Organophosphate Nerve Agents. Biochemistry V. 51 6463 2012.
ISSN: ISSN 0006-2960
PubMed: 22809162
DOI: 10.1021/BI300811T
Page generated: Tue Jul 30 16:42:49 2024
|