D-AMINO ACIC OXIDASE IN COMPLEX WITH D-ALANINE AND A PARTIALLY OCCUPIED BIATOMIC SPECIES
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). 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):
This entry contains 1 unique UniProt protein: