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Nickel in PDB 6g7r: Structure of Fully Reduced Variant E28Q of E. Coli Hydrogenase-1 at pH 8

Enzymatic activity of Structure of Fully Reduced Variant E28Q of E. Coli Hydrogenase-1 at pH 8

All present enzymatic activity of Structure of Fully Reduced Variant E28Q of E. Coli Hydrogenase-1 at pH 8:
1.12.99.6;

Protein crystallography data

The structure of Structure of Fully Reduced Variant E28Q of E. Coli Hydrogenase-1 at pH 8, PDB code: 6g7r 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) 67.89 / 1.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 94.068, 97.814, 183.210, 90.00, 90.00, 90.00
R / Rfree (%) 11.1 / 13.3

Other elements in 6g7r:

The structure of Structure of Fully Reduced Variant E28Q of E. Coli Hydrogenase-1 at pH 8 also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Iron (Fe) 24 atoms
Chlorine (Cl) 4 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the Structure of Fully Reduced Variant E28Q of E. Coli Hydrogenase-1 at pH 8 (pdb code 6g7r). 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 Variant E28Q of E. Coli Hydrogenase-1 at pH 8, PDB code: 6g7r:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in 6g7r

Go back to Nickel Binding Sites List in 6g7r
Nickel binding site 1 out of 2 in the Structure of Fully Reduced Variant E28Q of E. Coli Hydrogenase-1 at pH 8


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 Variant E28Q of E. Coli Hydrogenase-1 at pH 8 within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Ni602

b:11.3
occ:1.00
NI L:EJ2602 0.0 11.3 1.0
H L:EJ2602 1.6 9.7 1.0
SG L:CYS576 2.1 13.5 1.0
SG L:CYS76 2.3 9.5 1.0
SG L:CYS79 2.3 9.5 1.0
SG L:CYS579 2.5 8.7 1.0
FE L:EJ2602 2.6 8.8 1.0
H L:CYS79 2.8 8.8 1.0
HB2 L:CYS76 3.1 8.5 1.0
CB L:CYS76 3.1 8.6 1.0
HB3 L:CYS76 3.1 8.7 1.0
CB L:CYS576 3.2 11.6 1.0
HB3 L:CYS576 3.3 11.8 1.0
HB2 L:CYS579 3.4 7.9 1.0
HB2 L:CYS576 3.4 11.4 1.0
HB3 L:CYS79 3.4 9.2 1.0
CB L:CYS79 3.5 9.3 1.0
CB L:CYS579 3.6 7.7 1.0
HB L:VAL78 3.7 10.4 1.0
C1 L:EJ2602 3.7 8.7 1.0
N L:CYS79 3.7 8.6 1.0
C2 L:EJ2602 3.8 8.1 1.0
H L:CYS579 3.9 7.7 1.0
HH12 L:ARG509 4.0 14.1 0.0
HD2 L:ARG509 4.0 11.7 1.0
CA L:CYS79 4.2 8.8 1.0
HB3 L:CYS579 4.2 8.0 1.0
C3 L:EJ2602 4.2 10.2 1.0
HB2 L:CYS79 4.3 9.4 1.0
NH1 L:ARG509 4.3 14.1 1.0
H L:VAL78 4.3 8.9 1.0
HE2 L:HIS83 4.4 8.9 0.0
CA L:CYS76 4.5 7.6 1.0
HG3 L:GLN28 4.5 14.7 1.0
N L:CYS579 4.6 7.5 1.0
CA L:CYS579 4.6 8.0 1.0
HH11 L:ARG509 4.6 14.1 0.0
CA L:CYS576 4.6 9.5 1.0
N1 L:EJ2602 4.6 9.2 1.0
CB L:VAL78 4.6 10.3 1.0
CZ L:ARG509 4.7 11.5 1.0
N2 L:EJ2602 4.7 9.4 1.0
HA L:CYS579 4.7 7.9 1.0
HA L:CYS76 4.8 7.6 1.0
NE L:ARG509 4.8 11.6 1.0
CD L:ARG509 4.8 11.7 1.0
HA L:CYS576 4.8 9.7 1.0
C L:VAL78 4.8 9.6 1.0
HB3 L:GLN28 4.9 12.8 1.0
HA L:CYS79 4.9 8.8 1.0
HG11 L:VAL78 4.9 11.8 1.0
O L:HOH703 5.0 30.0 0.1

Nickel binding site 2 out of 2 in 6g7r

Go back to Nickel Binding Sites List in 6g7r
Nickel binding site 2 out of 2 in the Structure of Fully Reduced Variant E28Q of E. Coli Hydrogenase-1 at pH 8


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 Variant E28Q of E. Coli Hydrogenase-1 at pH 8 within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Ni601

b:11.4
occ:1.00
NI M:EJ2601 0.0 11.4 1.0
H M:EJ2601 1.6 9.5 1.0
SG M:CYS576 2.1 13.1 1.0
SG M:CYS76 2.2 9.6 1.0
SG M:CYS79 2.3 9.5 1.0
SG M:CYS579 2.5 8.7 1.0
FE M:EJ2601 2.6 8.7 1.0
H M:CYS79 2.9 8.6 1.0
CB M:CYS76 3.1 9.0 1.0
HB2 M:CYS76 3.1 9.0 1.0
HB3 M:CYS76 3.1 8.9 1.0
CB M:CYS576 3.2 11.4 1.0
HB3 M:CYS576 3.3 11.5 1.0
HB2 M:CYS579 3.4 8.2 1.0
HB2 M:CYS576 3.4 10.8 1.0
HB3 M:CYS79 3.4 8.8 1.0
CB M:CYS79 3.5 8.5 1.0
CB M:CYS579 3.6 7.8 1.0
HB M:VAL78 3.7 10.9 1.0
C1 M:EJ2601 3.7 8.6 1.0
N M:CYS79 3.8 8.5 1.0
C2 M:EJ2601 3.8 8.8 1.0
H M:CYS579 3.9 7.9 1.0
HD2 M:ARG509 4.0 11.5 1.0
HH12 M:ARG509 4.0 14.8 0.0
CA M:CYS79 4.2 9.4 1.0
HB3 M:CYS579 4.2 7.8 1.0
C3 M:EJ2601 4.3 9.5 1.0
HB2 M:CYS79 4.3 8.7 1.0
NH1 M:ARG509 4.3 14.3 1.0
H M:VAL78 4.4 9.0 1.0
HE2 M:HIS83 4.4 9.6 0.0
CA M:CYS76 4.5 7.9 1.0
HG3 M:GLN28 4.5 14.8 1.0
N M:CYS579 4.6 8.1 1.0
HH11 M:ARG509 4.6 14.8 0.0
CA M:CYS579 4.6 8.0 1.0
CA M:CYS576 4.6 8.9 1.0
N1 M:EJ2601 4.6 8.8 1.0
CB M:VAL78 4.6 10.9 1.0
CZ M:ARG509 4.7 11.7 1.0
N2 M:EJ2601 4.7 8.6 1.0
HA M:CYS579 4.7 8.0 1.0
CD M:ARG509 4.7 11.4 1.0
HA M:CYS76 4.8 8.1 1.0
NE M:ARG509 4.8 12.3 1.0
HA M:CYS576 4.8 9.2 1.0
C M:VAL78 4.8 8.9 1.0
HD3 M:ARG509 4.9 11.6 1.0
HB3 M:GLN28 4.9 13.2 1.0
HA M:CYS79 4.9 9.1 1.0
HG11 M:VAL78 5.0 12.4 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 08:28:39 2024

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