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-hydroxy-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: 2012-01-18) |
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 Cited by PubMed: 8591036DOI: 10.1016/S0969-2126(01)00261-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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