Nickel in PDB 3myr: Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State
Enzymatic activity of Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State
All present enzymatic activity of Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State:
1.12.99.6;
Protein crystallography data
The structure of Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State, PDB code: 3myr
was solved by
H.Ogata,
P.Kellers,
W.Lubitz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.10
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
205.750,
216.960,
119.800,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
13.8 /
16.8
|
Other elements in 3myr:
The structure of Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State also contains other interesting chemical elements:
Nickel Binding Sites:
The binding sites of Nickel atom in the Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State
(pdb code 3myr). This binding sites where shown within
5.0 Angstroms radius around Nickel atom.
In total 4 binding sites of Nickel where determined in the
Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State, PDB code: 3myr:
Jump to Nickel binding site number:
1;
2;
3;
4;
Nickel binding site 1 out
of 4 in 3myr
Go back to
Nickel Binding Sites List in 3myr
Nickel binding site 1 out
of 4 in the Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State
Mono view
Stereo pair view
|
A full contact list of Nickel with other atoms in the Ni binding
site number 1 of Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ni2005
b:22.3
occ:1.00
|
NI
|
B:NFV2005
|
0.0
|
22.3
|
1.0
|
O4
|
B:NFV2005
|
1.9
|
20.0
|
1.0
|
SG
|
B:CYS1555
|
2.2
|
24.4
|
1.0
|
SG
|
B:CYS1061
|
2.3
|
23.9
|
1.0
|
SG
|
B:CYS1064
|
2.6
|
21.7
|
1.0
|
SG
|
B:CYS1558
|
2.6
|
20.1
|
1.0
|
FE
|
B:NFV2005
|
3.0
|
16.3
|
1.0
|
CB
|
B:CYS1061
|
3.0
|
22.1
|
1.0
|
CB
|
B:CYS1555
|
3.2
|
18.2
|
1.0
|
CB
|
B:CYS1558
|
3.6
|
16.8
|
1.0
|
N
|
B:CYS1064
|
3.7
|
19.3
|
1.0
|
CB
|
B:CYS1064
|
3.9
|
18.2
|
1.0
|
C3
|
B:NFV2005
|
4.0
|
20.9
|
1.0
|
C2
|
B:NFV2005
|
4.3
|
13.9
|
1.0
|
CA
|
B:CYS1064
|
4.3
|
20.5
|
1.0
|
N
|
B:CYS1558
|
4.3
|
16.1
|
1.0
|
C1
|
B:NFV2005
|
4.4
|
19.5
|
1.0
|
CB
|
B:VAL1063
|
4.4
|
21.9
|
1.0
|
CA
|
B:CYS1061
|
4.5
|
20.2
|
1.0
|
CA
|
B:CYS1558
|
4.5
|
17.7
|
1.0
|
CA
|
B:CYS1555
|
4.6
|
18.7
|
1.0
|
NH1
|
B:ARG1487
|
4.7
|
24.0
|
1.0
|
C
|
B:VAL1063
|
4.7
|
20.4
|
1.0
|
N
|
B:VAL1063
|
4.8
|
21.6
|
1.0
|
CD
|
B:ARG1487
|
4.8
|
14.6
|
1.0
|
N3
|
B:NFV2005
|
4.8
|
16.9
|
1.0
|
CZ
|
B:ARG1487
|
4.8
|
23.2
|
1.0
|
CG
|
B:GLU1014
|
4.8
|
20.6
|
1.0
|
NE
|
B:ARG1487
|
4.9
|
19.9
|
1.0
|
C
|
B:CYS1061
|
4.9
|
19.2
|
1.0
|
CA
|
B:VAL1063
|
4.9
|
18.7
|
1.0
|
|
Nickel binding site 2 out
of 4 in 3myr
Go back to
Nickel Binding Sites List in 3myr
Nickel binding site 2 out
of 4 in the Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State
Mono view
Stereo pair view
|
A full contact list of Nickel with other atoms in the Ni binding
site number 2 of Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ni2005
b:22.7
occ:1.00
|
NI
|
D:NFV2005
|
0.0
|
22.7
|
1.0
|
O4
|
D:NFV2005
|
1.9
|
19.3
|
1.0
|
SG
|
D:CYS1555
|
2.2
|
30.9
|
1.0
|
SG
|
D:CYS1061
|
2.2
|
29.6
|
1.0
|
SG
|
D:CYS1558
|
2.6
|
24.3
|
1.0
|
SG
|
D:CYS1064
|
2.7
|
24.6
|
1.0
|
FE
|
D:NFV2005
|
3.0
|
18.2
|
1.0
|
CB
|
D:CYS1061
|
3.0
|
25.7
|
1.0
|
CB
|
D:CYS1555
|
3.2
|
26.9
|
1.0
|
CB
|
D:CYS1558
|
3.6
|
25.5
|
1.0
|
N
|
D:CYS1064
|
3.7
|
25.5
|
1.0
|
CB
|
D:CYS1064
|
3.8
|
26.2
|
1.0
|
C3
|
D:NFV2005
|
4.0
|
18.7
|
1.0
|
C1
|
D:NFV2005
|
4.3
|
13.8
|
1.0
|
CA
|
D:CYS1064
|
4.4
|
26.0
|
1.0
|
CB
|
D:VAL1063
|
4.4
|
28.2
|
1.0
|
N
|
D:CYS1558
|
4.4
|
25.6
|
1.0
|
C2
|
D:NFV2005
|
4.4
|
17.3
|
1.0
|
CA
|
D:CYS1061
|
4.4
|
25.1
|
1.0
|
CA
|
D:CYS1558
|
4.5
|
25.8
|
1.0
|
CA
|
D:CYS1555
|
4.6
|
27.7
|
1.0
|
C
|
D:VAL1063
|
4.8
|
27.4
|
1.0
|
NH1
|
D:ARG1487
|
4.8
|
25.4
|
1.0
|
CG
|
D:GLU1014
|
4.8
|
24.4
|
1.0
|
N
|
D:VAL1063
|
4.8
|
25.8
|
1.0
|
C
|
D:CYS1061
|
4.9
|
25.1
|
1.0
|
CZ
|
D:ARG1487
|
4.9
|
26.0
|
1.0
|
CD
|
D:ARG1487
|
4.9
|
26.5
|
1.0
|
CA
|
D:VAL1063
|
4.9
|
25.8
|
1.0
|
NE
|
D:ARG1487
|
4.9
|
24.4
|
1.0
|
N3
|
D:NFV2005
|
4.9
|
15.4
|
1.0
|
|
Nickel binding site 3 out
of 4 in 3myr
Go back to
Nickel Binding Sites List in 3myr
Nickel binding site 3 out
of 4 in the Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State
Mono view
Stereo pair view
|
A full contact list of Nickel with other atoms in the Ni binding
site number 3 of Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Ni2005
b:22.1
occ:1.00
|
NI
|
F:NFV2005
|
0.0
|
22.1
|
1.0
|
O4
|
F:NFV2005
|
1.9
|
21.3
|
1.0
|
SG
|
F:CYS1061
|
2.2
|
29.8
|
1.0
|
SG
|
F:CYS1555
|
2.3
|
30.5
|
1.0
|
SG
|
F:CYS1064
|
2.6
|
25.3
|
1.0
|
SG
|
F:CYS1558
|
2.7
|
25.0
|
1.0
|
FE
|
F:NFV2005
|
3.0
|
18.9
|
1.0
|
CB
|
F:CYS1061
|
3.0
|
25.7
|
1.0
|
CB
|
F:CYS1555
|
3.2
|
24.7
|
1.0
|
CB
|
F:CYS1558
|
3.6
|
26.4
|
1.0
|
N
|
F:CYS1064
|
3.7
|
25.3
|
1.0
|
CB
|
F:CYS1064
|
3.8
|
24.3
|
1.0
|
C3
|
F:NFV2005
|
3.9
|
21.3
|
1.0
|
C2
|
F:NFV2005
|
4.3
|
18.9
|
1.0
|
CA
|
F:CYS1064
|
4.3
|
26.5
|
1.0
|
C1
|
F:NFV2005
|
4.3
|
18.9
|
1.0
|
CB
|
F:VAL1063
|
4.4
|
28.7
|
1.0
|
CA
|
F:CYS1061
|
4.5
|
25.4
|
1.0
|
N
|
F:CYS1558
|
4.5
|
26.9
|
1.0
|
CA
|
F:CYS1558
|
4.5
|
26.1
|
1.0
|
NH1
|
F:ARG1487
|
4.6
|
24.9
|
1.0
|
CA
|
F:CYS1555
|
4.6
|
26.1
|
1.0
|
N3
|
F:NFV2005
|
4.7
|
16.4
|
1.0
|
C
|
F:VAL1063
|
4.8
|
27.5
|
1.0
|
CG
|
F:GLU1014
|
4.8
|
26.1
|
1.0
|
N
|
F:VAL1063
|
4.8
|
27.4
|
1.0
|
CD
|
F:ARG1487
|
4.8
|
20.2
|
1.0
|
CZ
|
F:ARG1487
|
4.8
|
27.2
|
1.0
|
NE
|
F:ARG1487
|
4.9
|
24.9
|
1.0
|
C
|
F:CYS1061
|
4.9
|
25.9
|
1.0
|
CA
|
F:VAL1063
|
4.9
|
27.4
|
1.0
|
CB
|
F:GLU1014
|
5.0
|
25.1
|
1.0
|
|
Nickel binding site 4 out
of 4 in 3myr
Go back to
Nickel Binding Sites List in 3myr
Nickel binding site 4 out
of 4 in the Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State
Mono view
Stereo pair view
|
A full contact list of Nickel with other atoms in the Ni binding
site number 4 of Crystal Structure of [Nife] Hydrogenase From Allochromatium Vinosum in Its Ni-A State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Ni2005
b:20.5
occ:1.00
|
NI
|
H:NFV2005
|
0.0
|
20.5
|
1.0
|
O4
|
H:NFV2005
|
1.9
|
18.0
|
1.0
|
SG
|
H:CYS1061
|
2.2
|
23.4
|
1.0
|
SG
|
H:CYS1555
|
2.3
|
26.4
|
1.0
|
SG
|
H:CYS1064
|
2.5
|
24.1
|
1.0
|
SG
|
H:CYS1558
|
2.6
|
20.9
|
1.0
|
CB
|
H:CYS1061
|
3.0
|
21.3
|
1.0
|
FE
|
H:NFV2005
|
3.0
|
16.8
|
1.0
|
CB
|
H:CYS1555
|
3.3
|
23.7
|
1.0
|
CB
|
H:CYS1558
|
3.6
|
22.1
|
1.0
|
N
|
H:CYS1064
|
3.7
|
21.5
|
1.0
|
CB
|
H:CYS1064
|
3.8
|
21.3
|
1.0
|
C3
|
H:NFV2005
|
4.0
|
15.7
|
1.0
|
C2
|
H:NFV2005
|
4.2
|
19.1
|
1.0
|
CA
|
H:CYS1064
|
4.3
|
23.6
|
1.0
|
N
|
H:CYS1558
|
4.3
|
21.1
|
1.0
|
C1
|
H:NFV2005
|
4.3
|
22.3
|
1.0
|
CB
|
H:VAL1063
|
4.4
|
23.9
|
1.0
|
CA
|
H:CYS1061
|
4.5
|
20.9
|
1.0
|
CA
|
H:CYS1558
|
4.5
|
21.8
|
1.0
|
NH1
|
H:ARG1487
|
4.6
|
24.6
|
1.0
|
CA
|
H:CYS1555
|
4.7
|
24.6
|
1.0
|
N
|
H:VAL1063
|
4.7
|
22.4
|
1.0
|
C
|
H:VAL1063
|
4.7
|
24.1
|
1.0
|
CD
|
H:ARG1487
|
4.8
|
20.0
|
1.0
|
N3
|
H:NFV2005
|
4.9
|
13.6
|
1.0
|
CA
|
H:VAL1063
|
4.9
|
23.2
|
1.0
|
CG
|
H:GLU1014
|
4.9
|
22.9
|
1.0
|
C
|
H:CYS1061
|
4.9
|
23.7
|
1.0
|
CZ
|
H:ARG1487
|
4.9
|
25.2
|
1.0
|
NE
|
H:ARG1487
|
4.9
|
20.4
|
1.0
|
|
Reference:
H.Ogata,
P.Kellers,
W.Lubitz.
The Crystal Structure of the [Nife] Hydrogenase From the Photosynthetic Bacterium Allochromatium Vinosum: Characterization of the Oxidized Enzyme (Ni-A State). J.Mol.Biol. V. 402 428 2010.
ISSN: ISSN 0022-2836
PubMed: 20673834
DOI: 10.1016/J.JMB.2010.07.041
Page generated: Wed Oct 9 17:32:46 2024
|