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Ligands
Code Name Style Show Link
SF4 Iron/sulfur cluster
F3S Fe3-s4 cluster
H2S Hydrosulfuric acid
GOL Glycerol
NI Nickel (II) ion
MG Magnesium ion
FCO Carbonmonoxide-(dicyano) iron
PER Peroxide ion
Non-standard Residues
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Glycosylation
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Code : 1YQ9   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Structure of the unready oxidized form of [NiFe] hydrogenase
Release Data : 2005-04-19
Compound :
mol_id molecule chains synonym
1 Periplasmic [NiFe] hydrogenase small subunit A,B NiFe hydrogenlyase small chain
ec: 1.12.2.1
mol_id molecule chains synonym
2 Periplasmic [NiFe] hydrogenase large subunit H,I NiFe hydrogenlyase large chain
ec: 1.12.2.1
Source :
mol_id organism_scientific
1 Desulfovibrio gigas  (taxid:879)
strain: wild type
cellular_location: periplasm
mol_id organism_scientific
2 Desulfovibrio gigas  (taxid:879)
strain: wild type
cellular_location: periplasm
Authors : Volbeda, A., Martin, L., Cavazza, C., Matho, M., Faber, B.W., Roseboom, W., Albracht, S.P., Garcin, E., Rousset, M., Fontecilla-Camps, J.C.
Keywords : oxidoreductase
Exp. method : X-RAY DIFFRACTION ( 2.35 Å )
Citation :

Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases.

Volbeda, A.,Martin, L.,Cavazza, C.  et al.
(2005)  J.Biol.Inorg.Chem.  10 : 239 - 249

PubMed: 15803334
DOI: 10.1007/s00775-005-0632-x

Structure of the [NiFe] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands

Volbeda, A.,Garcin, E.,Piras, C.  et al.
(1996)  J.Am.Chem.Soc.  118 : 12989 - 12996

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

Chain : A, B
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 -
-
Chain : H, I
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 -
-