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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:

Magnesium (Mg) 2 atoms
Iron (Fe) 24 atoms
Chlorine (Cl) 6 atoms

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

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