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PDBe Entry: 1eag 
SECRETED ASPARTIC PROTEINASE (SAP2) FROM CANDIDA ALBICANS COMPLEXED WITH A70450
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HYDROLASE (ASPARTIC PROTEASE)
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X-RAY DIFFRACTION
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Resolution: 2.1 Å, R-factor: 19.5%, Free R-factor: 26.8%, Spacegroup: P 43 21 2
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23/12/1996, deposition: 31/05/1996, last revision: 24/02/2009
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Cutfield, J.F.; Cutfield, S.M.
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The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors.
STRUCTURE vol:3, pag:1261-1271 (1995) [PubMed ID 8591036 ]
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SAP2, CANDIDA ALBICANS, HYDROLASE (ASPARTIC PROTEASE)
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3.4.23.24 ExPASy BRENDA (A)
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Candida albicans 5476(A)
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Candidapepsin-2 precursor (EC 3.4.23.24) (Aspartate protease 2) (ACP 2) (Secreted aspartic protease 2) P28871 (A)
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A
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| A |
ASPARTIC PROTEINASE (SAP2 GENE PRODUCT) |
Protein |
P28871 (CARP2_CANAL)
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342 |
99% |
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| A |
4-METHYLPIPERAZIN-1-YL CARBONYL GROUP |
ODS
PSS
LYW
CHA
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| A |
2,3-DIMETHYL-BUTYRALDEHYDE |
VAS
LYT
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