1c0p Summary



The structure was published by Umhau, S., Pollegioni, L., Molla, G., et al., Welte, W., Pilone, M.S., and Ghisla, S., in 2000 in a paper entitled "The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.2 Å and deposited in 1999.

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

The PDB entry contains the structure of D-AMINO ACID OXIDASE. This molecule has the UniProt identifier P80324 (OXDA_RHOTO)search. The sample contained 363 residues which is 98% of the natural sequence. Out of 363 residues 363 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 D-AMINO ACID OXIDASE P80324 (1-361) (OXDA_RHOTO)search Rhodosporidium toruloidessearch 98% 363 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P80324 (1 - 361) D-AMINO ACID OXIDASE Rhodosporidium toruloides

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P80324) D-aminoacid oxidase, N-terminal domainsearch, D-aminoacid oxidase-likesearch NAD(P)-binding Rossmann-like Domainsearch, D-Amino Acid Oxidase, subunit A, domain 2search PF01266: FAD dependent oxidoreductasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P80324) D-amino-acid oxidase activitysearch oxidoreductase activitysearch oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptorsearch oxidation-reduction processsearch peroxisomesearch

Chain InterPro annotation
A FAD dependent oxidoreductasesearch D-amino acid oxidase, conserved sitesearch D-amino-acid oxidasesearch