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3APR

BINDING OF A REDUCED PEPTIDE INHIBITOR TO THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS. IMPLICATIONS FOR A MECHANISM OF ACTION

Functional Information from GO Data
ChainGOidnamespacecontents
E0004190molecular_functionaspartic-type endopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR CHAIN I OF REDUCED PEPTIDE INHIBITOR
ChainResidue
EASP79
ESER81
EPHE114
ETRP194
EASP218
EGLY220
ETHR221
ETHR222
EILE225
ETRP294
EILE298
IHOH578
IHOH874
IHOH876
IHOH877
EGLU16
EASP33
EASP35
EGLY37
ESER76
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

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PDB entries from 2024-03-27

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