1EAG

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

1EAG の概要

• エントリーDOI: 10.2210/pdb1eag/pdb
• 分子名称: 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)
• 機能のキーワード: sap2, candida albicans, hydrolase-hydrolase inhibitor complex, aspartic protease, hydrolase/hydrolase inhibitor
• 由来する生物種: Candida albicans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37096.76

構造登録者

Cutfield, J.F.,Cutfield, S.M. (登録日: 1996-05-31, 公開日: 1996-12-23, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)