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THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS PLANTARUM

The structure was published by Muller, Y.A., Schumacher, G., Rudolph, R., and Schulz, G.E., in 1994 in a paper entitled "The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1993.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of PYRUVATE OXIDASE.

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 homotetramers.

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 PYRUVATE OXIDASE P37063 (9-593) (POXB_LACPL)search Lactobacillus plantarum WCFS1search 97% 585 100%
B PYRUVATE OXIDASE P37063 (9-593) (POXB_LACPL)search Lactobacillus plantarum WCFS1search 97% 585 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P37063 (9 - 593) PYRUVATE OXIDASE Lactobacillus plantarum

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P37063) Pyruvate oxidase and decarboxylase, middle domainsearch, Pyruvate oxidase and decarboxylase Pyr modulesearch, Pyruvate oxidase and decarboxylase PP modulesearch Rossmann foldsearch, TPP-binding domainsearch PF00205: Thiamine pyrophosphate enzyme, central domainsearch, PF02775: Thiamine pyrophosphate enzyme, C-terminal TPP binding domainsearch, PF02776: Thiamine pyrophosphate enzyme, N-terminal TPP binding domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (P37063) oxidation-reduction processsearch thiamine pyrophosphate bindingsearch magnesium ion bindingsearch catalytic activitysearch pyruvate oxidase activitysearch metal ion bindingsearch oxidoreductase activitysearch

Chain InterPro annotation
A, B TPP-binding enzyme, conserved sitesearch Thiamine pyrophosphate enzyme, C-terminal TPP-bindingsearch Thiamine pyrophosphate enzyme, central domainsearch Thiamine pyrophosphate enzyme, N-terminal TPP-binding domainsearch Pyruvate oxidasesearch DHS-like NAD/FAD-binding domainsearch Thiamin diphosphate-binding foldsearch