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1MT8

Viability of a drug-resistant HIV-1 protease mutant: structural insights for better antiviral therapy

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 Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 501
ChainResidue
APRO1
BHIS69
BLYS70

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 503
ChainResidue
AARG14
AGLY16
BARG14
BGLY16

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT P 508
ChainResidue
PALA2
PARG3

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR CHAIN P OF CAPSID-P2 SUBSTRATE PEPTIDE OF HIV-1 GAG POLYPROTEIN
ChainResidue
AARG8
AASN25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AILE84
BASN25
BGLY27
BALA28
BASP29
BASP30
BILE47
BGLY48
BGLY49
BPRO81
PACT508
PHOH510
PHOH512

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues138
DetailsDomain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASN25
ATHR26
BASN25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASN25
BASN25

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PDB entries from 2025-12-17

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