1EAG

Secreted aspartic proteinase (SAP2) from Candida albicans complexed with A70450

Summary for 1EAG

• Entry DOI: 10.2210/pdb1eag/pdb
• Descriptor: ASPARTIC PROTEINASE (SAP2 GENE PRODUCT), N-ethyl-N-[(4-methylpiperazin-1-yl)carbonyl]-D-phenylalanyl-N-[(1S,2S,4R)-4-(butylcarbamoyl)-1-(cyclohexylmethyl)-2-hyd roxy-5-methylhexyl]-L-norleucinamide (3 entities in total)
• Functional Keywords: sap2, candida albicans, hydrolase-hydrolase inhibitor complex, aspartic protease, hydrolase/hydrolase inhibitor
• Biological source: Candida albicans
• Total number of polymer chains: 1
• Total formula weight: 37096.76

Authors

Cutfield, J.F.,Cutfield, S.M. (deposition date: 1996-05-31, release date: 1996-12-23, Last modification date: 2024-10-30)

Primary citation

Cutfield, S.M.,Dodson, E.J.,Anderson, B.F.,Moody, P.C.E.,Marshall, C.J.,Sullivan, P.A.,Cutfield, J.F.
The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors.
Structure, 3:1261-1271, 1995

PubMed Abstract: Infections caused by Candida albicans, a common fungal pathogen of humans, are increasing in incidence, necessitating development of new therapeutic drugs. Secreted aspartic proteinase (SAP) activity is considered an important virulence factor in these infections and might offer a suitable target for drug design. Amongst the various SAP isozymes, the SAP2 gene product is the major form expressed in a number of C. albicans strains.

PubMed: 8591036
DOI: 10.1016/S0969-2126(01)00261-1

Experimental method

X-RAY DIFFRACTION (2.1 Å)