2pda Summary



The structure was published by Chabriere, E., Charon, M.H., Volbeda, A., Pieulle, L., Hatchikian, E.C., and Fontecilla-Camps, J.C., in 1999 in a paper entitled "Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of PROTEIN (PYRUVATE-FERREDOXIN OXIDOREDUCTASE).

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PROTEIN (PYRUVATE-FERREDOXIN OXIDOREDUCTASE) P94692 (2-1232) (POR_DESAF)search Desulfovibrio africanussearch 100% 1231 100%
B PROTEIN (PYRUVATE-FERREDOXIN OXIDOREDUCTASE) P94692 (2-1232) (POR_DESAF)search Desulfovibrio africanussearch 100% 1231 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P94692 (2 - 1232) PROTEIN (PYRUVATE-FERREDOXIN OXIDOREDUCTASE) Desulfovibrio africanus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P94692) PFOR Pyr modulesearch, PFOR PP modulesearch, Pyruvate-ferredoxin oxidoreductase, PFOR, domain IIsearch, Pyruvate-ferredoxin oxidoreductase, PFOR, domain IIIsearch, Ferredoxin domains from multidomain proteinssearch Rossmann foldsearch, Pyruvate-ferredoxin oxidoreductase, PFOR, domain IIIsearch, Pyruvate-ferredoxin Oxidoreductase; domain 4search, Alpha-Beta Plaitssearch, Pyruvate-ferredoxin Oxidoreductase; domain 7search PF00037: 4Fe-4S binding domainsearch, PF01558: Pyruvate ferredoxin/flavodoxin oxidoreductasesearch, PF01855: Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdgsearch, PF02775: Thiamine pyrophosphate enzyme, C-terminal TPP binding domainsearch, PF10371: Domain of unknown functionsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P94692) iron ion bindingsearch iron-sulfur cluster bindingsearch thiamine pyrophosphate bindingsearch oxidoreductase activity, acting on the aldehyde or oxo group of donorssearch catalytic activitysearch 4 iron, 4 sulfur cluster bindingsearch oxidoreductase activitysearch metal ion bindingsearch pyruvate synthase activitysearch oxidation-reduction processsearch acetyl-CoA biosynthetic process from pyruvatesearch metabolic processsearch electron transport chainsearch cytoplasmsearch

Chain InterPro annotation
A, B 4Fe-4S binding domainsearch Pyruvate-flavodoxin oxidoreductase, central domainsearch Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminalsearch Transketolase, C-terminal/Pyruvate-ferredoxin oxidoreductase, domain IIsearch Thiamine pyrophosphate enzyme, C-terminal TPP-bindingsearch Pyruvate-flavodoxin oxidoreductasesearch 4Fe-4S ferredoxin-type, iron-sulphur binding domainsearch 4Fe-4S ferredoxin, iron-sulphur binding, conserved sitesearch Pyruvate-flavodoxin oxidoreductase, EKR domainsearch Pyruvate/ketoisovalerate oxidoreductase, catalytic domainsearch Thiamin diphosphate-binding foldsearch