Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450
The structure was published by Cutfield, S.M., Dodson, E.J., Anderson, B.F., et al., Marshall, C.J., Sullivan, P.A., and Cutfield, J.F., in 1995 in a paper entitled "The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1996.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of ASPARTIC PROTEINASE (SAP2 GENE PRODUCT). This molecule has the UniProt identifier P0CS83 (CARP2_CANAX). The sample contained 342 residues which is 90% of the natural sequence. Out of 342 residues 339 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: