Nickel in PDB 6fpi: Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q
Enzymatic activity of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q
All present enzymatic activity of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q:
1.12.99.6;
Protein crystallography data
The structure of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q, PDB code: 6fpi
was solved by
S.B.Carr,
F.A.Armstrong,
R.M.Evans,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
83.51 /
1.50
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
93.820,
97.730,
183.200,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
14.5 /
16.7
|
Other elements in 6fpi:
The structure of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q also contains other interesting chemical elements:
Nickel Binding Sites:
The binding sites of Nickel atom in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q
(pdb code 6fpi). This binding sites where shown within
5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the
Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q, PDB code: 6fpi:
Jump to Nickel binding site number:
1;
2;
Nickel binding site 1 out
of 2 in 6fpi
Go back to
Nickel Binding Sites List in 6fpi
Nickel binding site 1 out
of 2 in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q
Mono view
Stereo pair view
|
A full contact list of Nickel with other atoms in the Ni binding
site number 1 of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Ni601
b:16.4
occ:1.00
|
NI
|
L:EJ2601
|
0.0
|
16.4
|
1.0
|
H
|
L:EJ2601
|
1.6
|
14.5
|
1.0
|
SG
|
L:CYS576
|
2.1
|
22.4
|
1.0
|
SG
|
L:CYS79
|
2.3
|
15.9
|
1.0
|
SG
|
L:CYS76
|
2.3
|
16.5
|
1.0
|
SG
|
L:CYS579
|
2.5
|
15.2
|
1.0
|
FE
|
L:EJ2601
|
2.6
|
13.4
|
1.0
|
H
|
L:CYS79
|
2.9
|
15.8
|
1.0
|
CB
|
L:CYS76
|
3.1
|
14.9
|
1.0
|
HB2
|
L:CYS76
|
3.1
|
14.9
|
1.0
|
HB3
|
L:CYS76
|
3.1
|
14.9
|
1.0
|
CB
|
L:CYS576
|
3.2
|
17.9
|
1.0
|
HB2
|
L:CYS576
|
3.3
|
18.4
|
1.0
|
HB3
|
L:CYS576
|
3.3
|
18.4
|
1.0
|
HB3
|
L:CYS79
|
3.4
|
16.0
|
1.0
|
HB2
|
L:CYS579
|
3.4
|
14.4
|
1.0
|
CB
|
L:CYS79
|
3.4
|
16.1
|
1.0
|
CB
|
L:CYS579
|
3.6
|
14.3
|
1.0
|
C1
|
L:EJ2601
|
3.6
|
13.5
|
1.0
|
HB
|
L:VAL78
|
3.7
|
17.6
|
1.0
|
C2
|
L:EJ2601
|
3.7
|
14.0
|
1.0
|
N
|
L:CYS79
|
3.7
|
15.3
|
1.0
|
H
|
L:CYS579
|
3.9
|
13.4
|
1.0
|
HD2
|
L:ARG509
|
4.0
|
18.0
|
1.0
|
HH11
|
L:ARG509
|
4.1
|
19.8
|
1.0
|
CA
|
L:CYS79
|
4.1
|
16.0
|
1.0
|
C3
|
L:EJ2601
|
4.2
|
11.8
|
1.0
|
HB2
|
L:CYS79
|
4.2
|
16.0
|
1.0
|
HB3
|
L:CYS579
|
4.2
|
14.4
|
1.0
|
NH1
|
L:ARG509
|
4.3
|
20.3
|
1.0
|
H
|
L:VAL78
|
4.4
|
14.8
|
1.0
|
HE2
|
L:HIS83
|
4.5
|
14.6
|
0.0
|
N1
|
L:EJ2601
|
4.6
|
14.3
|
1.0
|
HH12
|
L:ARG509
|
4.6
|
19.9
|
1.0
|
HG3
|
L:GLN28
|
4.6
|
23.9
|
1.0
|
CA
|
L:CYS76
|
4.6
|
13.7
|
1.0
|
CA
|
L:CYS576
|
4.6
|
16.1
|
1.0
|
CA
|
L:CYS579
|
4.6
|
13.6
|
1.0
|
CB
|
L:VAL78
|
4.6
|
17.4
|
1.0
|
N
|
L:CYS579
|
4.6
|
13.5
|
1.0
|
N2
|
L:EJ2601
|
4.7
|
13.7
|
1.0
|
CZ
|
L:ARG509
|
4.7
|
19.0
|
1.0
|
CD
|
L:ARG509
|
4.7
|
18.1
|
1.0
|
HG11
|
L:VAL78
|
4.7
|
18.2
|
1.0
|
HA
|
L:CYS576
|
4.8
|
16.2
|
1.0
|
HA
|
L:CYS579
|
4.8
|
13.7
|
1.0
|
C
|
L:VAL78
|
4.8
|
16.8
|
1.0
|
HA
|
L:CYS76
|
4.8
|
13.7
|
1.0
|
NE
|
L:ARG509
|
4.8
|
18.1
|
1.0
|
HA
|
L:CYS79
|
4.9
|
15.9
|
1.0
|
HD3
|
L:ARG509
|
5.0
|
18.0
|
1.0
|
HB3
|
L:GLN28
|
5.0
|
21.0
|
1.0
|
|
Nickel binding site 2 out
of 2 in 6fpi
Go back to
Nickel Binding Sites List in 6fpi
Nickel binding site 2 out
of 2 in the Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q
Mono view
Stereo pair view
|
A full contact list of Nickel with other atoms in the Ni binding
site number 2 of Structure of Fully Reduced Hydrogenase (Hyd-1) Variant E28Q within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Ni601
b:16.4
occ:1.00
|
NI
|
M:EJ2601
|
0.0
|
16.4
|
1.0
|
H
|
M:EJ2601
|
1.6
|
14.8
|
1.0
|
SG
|
M:CYS576
|
2.1
|
22.3
|
1.0
|
SG
|
M:CYS76
|
2.2
|
16.4
|
1.0
|
SG
|
M:CYS79
|
2.3
|
16.7
|
1.0
|
SG
|
M:CYS579
|
2.5
|
15.3
|
1.0
|
FE
|
M:EJ2601
|
2.6
|
13.7
|
1.0
|
H
|
M:CYS79
|
2.8
|
14.6
|
1.0
|
CB
|
M:CYS76
|
3.1
|
14.8
|
1.0
|
HB2
|
M:CYS76
|
3.1
|
14.9
|
1.0
|
HB3
|
M:CYS76
|
3.1
|
14.9
|
1.0
|
CB
|
M:CYS576
|
3.2
|
17.8
|
1.0
|
HB2
|
M:CYS576
|
3.3
|
18.2
|
1.0
|
HB3
|
M:CYS576
|
3.4
|
18.2
|
1.0
|
HB2
|
M:CYS579
|
3.4
|
14.4
|
1.0
|
HB3
|
M:CYS79
|
3.4
|
15.3
|
1.0
|
CB
|
M:CYS79
|
3.5
|
14.8
|
1.0
|
CB
|
M:CYS579
|
3.6
|
14.2
|
1.0
|
HB
|
M:VAL78
|
3.6
|
17.2
|
1.0
|
C1
|
M:EJ2601
|
3.7
|
14.6
|
1.0
|
N
|
M:CYS79
|
3.7
|
13.6
|
1.0
|
C2
|
M:EJ2601
|
3.8
|
13.9
|
1.0
|
H
|
M:CYS579
|
3.9
|
14.2
|
1.0
|
HD2
|
M:ARG509
|
4.0
|
17.8
|
1.0
|
HH11
|
M:ARG509
|
4.1
|
21.0
|
1.0
|
CA
|
M:CYS79
|
4.2
|
15.0
|
1.0
|
C3
|
M:EJ2601
|
4.2
|
12.1
|
1.0
|
HB2
|
M:CYS79
|
4.2
|
15.3
|
1.0
|
HB3
|
M:CYS579
|
4.2
|
14.4
|
1.0
|
NH1
|
M:ARG509
|
4.3
|
21.4
|
1.0
|
H
|
M:VAL78
|
4.4
|
15.0
|
1.0
|
HE2
|
M:HIS83
|
4.5
|
14.8
|
0.0
|
HG3
|
M:GLN28
|
4.6
|
23.4
|
1.0
|
HH12
|
M:ARG509
|
4.6
|
21.1
|
1.0
|
CA
|
M:CYS76
|
4.6
|
13.7
|
1.0
|
N
|
M:CYS579
|
4.6
|
14.7
|
1.0
|
CB
|
M:VAL78
|
4.6
|
17.6
|
1.0
|
CA
|
M:CYS576
|
4.6
|
15.6
|
1.0
|
CA
|
M:CYS579
|
4.6
|
13.8
|
1.0
|
N1
|
M:EJ2601
|
4.6
|
14.9
|
1.0
|
N2
|
M:EJ2601
|
4.7
|
13.0
|
1.0
|
HA
|
M:CYS576
|
4.7
|
16.0
|
1.0
|
CZ
|
M:ARG509
|
4.7
|
20.7
|
1.0
|
HA
|
M:CYS579
|
4.8
|
14.1
|
1.0
|
CD
|
M:ARG509
|
4.8
|
18.1
|
1.0
|
HA
|
M:CYS76
|
4.8
|
13.9
|
1.0
|
C
|
M:VAL78
|
4.8
|
16.4
|
1.0
|
NE
|
M:ARG509
|
4.9
|
18.3
|
1.0
|
HG11
|
M:VAL78
|
4.9
|
17.6
|
1.0
|
HA
|
M:CYS79
|
4.9
|
15.0
|
1.0
|
HB3
|
M:GLN28
|
4.9
|
21.7
|
1.0
|
HD3
|
M:ARG509
|
5.0
|
17.8
|
1.0
|
|
Reference:
R.M.Evans,
P.A.Ash,
S.E.Beaton,
E.J.Brooke,
K.A.Vincent,
S.B.Carr,
F.A.Armstrong.
Mechanistic Exploitation of A Self-Repairing, Blocked Proton Transfer Pathway in An O2-Tolerant [Nife]-Hydrogenase. J. Am. Chem. Soc. V. 140 10208 2018.
ISSN: ESSN 1520-5126
PubMed: 30070475
DOI: 10.1021/JACS.8B04798
Page generated: Thu Oct 10 08:27:17 2024
|