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). 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):
This entry contains 1 unique UniProt protein: