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1EAG

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

Summary for 1EAG
Entry DOI10.2210/pdb1eag/pdb
DescriptorASPARTIC 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 Keywordssap2, candida albicans, hydrolase-hydrolase inhibitor complex, aspartic protease, hydrolase/hydrolase inhibitor
Biological sourceCandida albicans
Total number of polymer chains1
Total formula weight37096.76
Authors
Cutfield, J.F.,Cutfield, S.M. (deposition date: 1996-05-31, release date: 1996-12-23, Last modification date: 2012-01-18)
Primary citationCutfield, 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: 8591036
DOI: 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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