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PDBsum entry 4ttt

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
4ttt

 

 

 

 

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Contents
Protein chains
598 a.a.
269 a.a.
Ligands
NFV
PO4
SF4
F3S
F4S
Metals
_NA
_CL ×3
_MG
Waters ×614
PDB id:
4ttt
Name: Oxidoreductase
Title: Crystal structure of an o2-tolerant [nife]-hydrogenase from ralstonia eutropha in its as-isolated form - oxidized state 3
Structure: Uptake hydrogenase large subunit hoxg. Chain: l. Fragment: unp residues 1-603. Synonym: hydrogenlyase,membrane-bound hydrogenase large subunit. Engineered: yes. Uptake hydrogenase small subunit hoxk. Chain: s. Fragment: residues 44-360. Synonym: hydrogenlyase,membrane-bound hydrogenase small subunit.
Source: Ralstonia eutropha. Organism_taxid: 381666. Strain: atcc 17699 / h16 / dsm 428 / stanier 337. Atcc: 17699. Gene: hoxg, phg002. Expressed in: ralstonia eutropha. Expression_system_taxid: 381666. Expression_system_atcc_number: 17699. Gene: hoxk, phg001.
Resolution:
1.72Å     R-factor:   0.136     R-free:   0.165
Authors: A.Schmidt,J.Kalms,P.Scheerer
Key ref: A.Schmidt et al. Crystal structure of an o2-Tolerant [nife]-Hydrogenas ralstonia eutropha in its as-Isolated form (oxidized - 3. To be published, .
Date:
23-Jun-14     Release date:   28-Jan-15    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P31891  (MBHL_CUPNH) -  Uptake hydrogenase large subunit from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
Seq:
Struc:
 
Seq:
Struc:
618 a.a.
598 a.a.
Protein chain
Pfam   ArchSchema ?
P31892  (MBHS_CUPNH) -  Uptake hydrogenase small subunit from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
Seq:
Struc:
360 a.a.
269 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains L, S: E.C.1.12.99.6  - hydrogenase (acceptor).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: H2 + A = AH2
      Cofactor: Iron-sulfur; Ni(2+)
Iron-sulfur
Ni(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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