1bfd Summary

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BENZOYLFORMATE DECARBOXYLASE FROM PSEUDOMONAS PUTIDA

The structure was published by Hasson, M.S., Muscate, A., McLeish, M.J., et al., Kenyon, G.L., Petsko, G.A., and Ringe, D., in 1998 in a paper entitled "The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 1998.

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

The PDB entry contains the structure of BENZOYLFORMATE DECARBOXYLASE. This molecule has the UniProt identifier P20906 (MDLC_PSEPU)search. The sample contained 528 residues which is 100% of the natural sequence. Out of 528 residues 523 were observed and are deposited in the PDB.

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 BENZOYLFORMATE DECARBOXYLASE P20906 (1-528) (MDLC_PSEPU)search Pseudomonas putidasearch 99% 528 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P20906 (1 - 528) BENZOYLFORMATE DECARBOXYLASE Pseudomonas putida

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P20906) Pyruvate oxidase and decarboxylase, middle domainsearch, Pyruvate oxidase and decarboxylase Pyr modulesearch, Pyruvate oxidase and decarboxylase PP modulesearch TPP-binding domainsearch, Rossmann foldsearch 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 Molecular function (GO) Biological process (GO)
A (P20906) thiamine pyrophosphate bindingsearch magnesium ion bindingsearch catalytic activitysearch metal ion bindingsearch carboxy-lyase activitysearch lyase activitysearch benzoylformate decarboxylase activitysearch aromatic compound catabolic processsearch mandelate metabolic processsearch mandelate catabolic processsearch

Chain InterPro annotation
A 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 DHS-like NAD/FAD-binding domainsearch Thiamin diphosphate-binding foldsearch