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Nickel in PDB 1wul: High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F

Enzymatic activity of High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F

All present enzymatic activity of High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F:
1.12.2.1;

Protein crystallography data

The structure of High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F, PDB code: 1wul was solved by H.Ogata, S.Hirota, A.Nakahara, H.Komori, N.Shibata, T.Kato, K.Kano, Y.Higuchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 98.116, 126.016, 66.731, 90.00, 90.00, 90.00
R / Rfree (%) 12.2 / 16.9

Nickel Binding Sites:

The binding sites of Nickel atom in the High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F (pdb code 1wul). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F, PDB code: 1wul:

Nickel binding site 1 out of 1 in 1wul

Go back to Nickel Binding Sites List in 1wul
Nickel binding site 1 out of 1 in the High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of High Resolution Structure of the Reduced State of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Ni1004

b:8.3
occ:0.96
NI L:NFR1004 0.0 8.3 1.0
SG L:CSO546 2.1 9.6 1.0
SG L:CYS81 2.2 8.1 0.9
SG L:CYS84 2.2 8.5 1.0
SG L:CYS549 2.5 8.3 1.0
FE L:NFR1004 2.6 8.0 1.0
OD L:CSO546 3.0 15.4 0.8
CB L:CYS81 3.1 10.2 1.0
CB L:CSO546 3.3 9.1 1.0
CB L:CYS84 3.3 8.0 1.0
CB L:CYS549 3.6 6.8 1.0
N L:CYS84 3.7 7.9 1.0
C2 L:NFR1004 3.7 6.7 1.0
C1 L:NFR1004 3.8 7.3 1.0
CA L:CYS84 4.1 7.5 1.0
C3 L:NFR1004 4.2 7.7 1.0
NH1 L:ARG479 4.3 8.7 1.0
CA L:CYS81 4.5 7.4 1.0
CD L:ARG479 4.6 8.2 1.0
CB L:VAL83 4.6 8.0 1.0
O1 L:NFR1004 4.6 13.0 1.0
CA L:CSO546 4.6 7.5 1.0
CZ L:ARG479 4.6 7.0 1.0
CA L:CYS549 4.7 7.1 1.0
N L:CYS549 4.7 7.4 1.0
N2 L:NFR1004 4.7 8.4 1.0
NE L:ARG479 4.7 6.6 1.0
C L:VAL83 4.8 7.9 1.0
C L:CYS84 4.8 7.5 1.0
O L:CYS84 5.0 9.0 1.0

Reference:

H.Ogata, S.Hirota, A.Nakahara, H.Komori, N.Shibata, T.Kato, K.Kano, Y.Higuchi. Activation Process of [Nife] Hydrogenase Elucidated By High-Resolution X-Ray Analyses: Conversion of the Ready to the Unready State Structure V. 13 1635 2005.
ISSN: ISSN 0969-2126
PubMed: 16271886
DOI: 10.1016/J.STR.2005.07.018
Page generated: Fri Sep 25 08:03:47 2020
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