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4APR

STRUCTURES OF COMPLEXES OF RHIZOPUSPEPSIN WITH PEPSTATIN AND OTHER STATINE-CONTAINING INHIBITORS

Functional Information from GO Data
ChainGOidnamespacecontents
E0004190molecular_functionaspartic-type endopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR CHAIN I OF PEPSTATIN-LIKE RENIN INHIBITOR
ChainResidue
EASP79
ESER81
EASP218
EGLY220
ETHR221
ETHR222
ETRP294
IHOH578
IHOH884
EILE15
EGLU16
EASP33
EASP35
EGLY37
ETYR77
EGLY78

site_idCAT
Number of Residues2
DetailsCATALYTICALLY ACTIVE RESIDUES
ChainResidue
EASP35
EASP218

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LDFDTGSSDLWI
ChainResidueDetails
ELEU32-ILE43
EGLY215-LEU226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
EASP35
EASP218

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP35

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP218

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ETHR221
ESER38
EASP35
EASP218

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP35
EASP218
ETHR219
ETHR36

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ESER38
EASP35
EASP218

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ESER38
EASP35
EASP218
ETYR77

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
ETHR221
EASP35
EASP218
ETHR36

237735

PDB entries from 2025-06-18

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