Brand  (β version)

PDB ID: 1FRV

Hetero Atom Contents

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Code Name Style Show Link
SF4 Iron/sulfur cluster PoSSuM
F3S Fe3-s4 cluster PoSSuM
NI Nickel (II) ion PoSSuM
FE Fe (III) ion PoSSuM

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Structure summary

Code : 1FRV   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE
Release Data : 1996-11-08
Compound :
mol_id molecule chains synonym
1 HYDROGENASE A,C CYTOCHROME-C3 HYDROGENASE
ec: 1.12.2.1
mol_id molecule chains synonym
2 HYDROGENASE B,D CYTOCHROME-C3 HYDROGENASE
ec: 1.12.2.1
Source :
mol_id organism_scientific
1 Desulfovibrio gigas  (taxid:879)
atcc: 19364
mol_id organism_scientific
2 Desulfovibrio gigas  (taxid:879)
atcc: 19364
Authors : Volbeda, A., Frey, M., Fontecilla-Camps, J.C.
Keywords : NI-FE HYDROGENASE, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.85 Å )
Citation :

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.

Volbeda, A.,Charon, M.H.,Piras, C.  et al.
(1995)  Nature  373 : 580 - 587

PubMed: 7854413
DOI: 10.1038/373580a0

Location of the Redox Centers in Hydrogenase as Determined by X-Ray Crystallography at 5 Angstroms Resolution

Volbeda, A.,Piras, C.,Charon, M.H.  et al.
(1993)  Joint Ccp4 Esf-Eacbm Newsletter on Protein Crystallography  28 : 30

Analysis and Comparison of Nucleotide Sequences Encoding the Genes for [Nife] and [Nifese] Hydrogenases from Desulfovibrio Gigas and Desulfovibrio Baculatus

Voordouw, G.,Menon, N.K.,Legall, J.  et al.
(1989)  J.Bacteriol.  171 : 2894

Reaction

Chain : A, C
UniProt : P12943 (PHNS_MEGGA)
Reaction: EC: Evidence:
Physiological Direction:
2 Fe(III)-[cytochrome c3] + H2 = 2 Fe(II)-[cytochrome c3] + 2 H(+) 1.12.2.1 -
-
Cofactor: Evidence: Note:
[4Fe-4S] cluster - Binds 2 [4Fe-4S] clusters.
[3Fe-4S] cluster - Binds 1 [3Fe-4S] cluster.
Chain : B, D
UniProt : P12944 (PHNL_MEGGA)
Reaction: EC: Evidence:
Physiological Direction:
2 Fe(III)-[cytochrome c3] + H2 = 2 Fe(II)-[cytochrome c3] + 2 H(+) 1.12.2.1 -
-
Cofactor: Evidence: Note:
Ni(2+) - Binds 1 nickel ion per subunit.