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3OTY

MDR769 HIV-1 protease complexed with RT/RH hepta-peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR CHAIN P OF RT/RH SUBSTRATE PEPTIDE
ChainResidue
AARG8
AHOH200
BARG8
BASN25
BGLY27
BALA28
BASP29
BARG41
BLYS45
BLEU46
BILE47
ALEU23
BGLY48
BVAL84
BHOH129
BHOH199
PHOH44
PHOH101
PHOH147
PHOH169
PHOH263
PHOH264
AASN25
PHOH271
PHOH277
AGLY27
AALA28
AASP29
AASP30
ATHR82
AHOH195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues20
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Cleavage; by viral protease; partial","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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