1g79 Summary

pdbe.org/1g79
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X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE OXIDASE COMPLEXED WITH PYRIDOXAL 5'-PHOSPHATE AT 2.0 A RESOLUTION

The structure was published by Safo, M.K., Musayev, F.N., di Salvo, M.L., and Schirch, V., in 2001 in a paper entitled "X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with pyridoxal 5'-phosphate at 2.0 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2000.

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

The PDB entry contains the structure of PYRIDOXINE 5'-PHOSPHATE OXIDASE. This molecule has the UniProt identifier P0AFI7 (PDXH_ECOLI)search. The sample contained 218 residues which is 100% of the natural sequence. Out of 218 residues 199 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 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 PYRIDOXINE 5'-PHOSPHATE OXIDASE P0AFI7 (1-218) (PDXH_ECOLI)search Escherichia coli K-12search 91% 218 91%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0AFI7 (1 - 218) PYRIDOXINE 5'-PHOSPHATE OXIDASE Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P0AFI7) PNP-oxidase likesearch Electron Transport, Fmn-binding Protein; Chain Asearch PF01243: Pyridoxamine 5'-phosphate oxidasesearch, PF10590: Pyridoxine 5'-phosphate oxidase C-terminal dimerisation regionsearch

Chain ID Biological process (GO) Molecular function (GO)
A (P0AFI7) oxidation-reduction processsearch pyridoxine biosynthetic processsearch vitamin B6 metabolic processsearch pyridoxal 5'-phosphate salvagesearch FMN bindingsearch oxidoreductase activity, acting on the CH-NH2 group of donorssearch pyridoxamine-phosphate oxidase activitysearch oxidoreductase activitysearch

Chain InterPro annotation
A Pyridoxamine 5'-phosphate oxidasesearch Pyridoxamine 5'-phosphate oxidase-like, FMN-binding domainsearch FMN-binding split barrelsearch Pyridoxine 5'-phosphate oxidase, dimerisation, C-terminalsearch Pyridoxamine 5'-phosphate oxidase, conserved sitesearch