CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA COMPLEXED WITH CITRATE
The structure was published by Pawelek, P.D., Cheah, J., Coulombe, R., Macheroux, P., Ghisla, S., and Vrielink, A., in 2000 in a paper entitled "The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site." (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.
This PDB entry contains multiple copies of the structure of L-AMINO ACID OXIDASE.
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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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: