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1YTJ

SIV PROTEASE CRYSTALLIZED WITH PEPTIDE PRODUCT

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR CHAIN I OF PEPTIDE PRODUCT
ChainResidue
APRO1
AILE46
AVAL47
AGLY48
APRO81
AILE82
AILE84
IHOH401
IHOH401
AARG8
ALEU23
AASP25
AASP25
AGLY27
AALA28
AASP29
AASP30

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VLLDTGADDSIV
ChainResidueDetails
AVAL22-VAL33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues69
DetailsDomain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Cleavage; by viral protease","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25

251422

PDB entries from 2026-04-01

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