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1MTB

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 Residues9
DetailsBINDING SITE FOR RESIDUE QNC A 100
ChainResidue
ATRP6
AGLY27
AALA28
AASP29
AGLY48
AASN101
AHPH102
AHOH113
BARG8

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ASN A 101
ChainResidue
AASP30
AILE47
AGLY48
AQNC100
AHPH102
AHOH103

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HPH A 102
ChainResidue
AASN25
AGLY27
AGLY49
AILE50
AQNC100
AASN101
BASN25
BPRO81
BDIQ100

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DIQ B 100
ChainResidue
AASN25
APRO81
AHPH102
AHOH103
BASN25
BGLY27
BNTB101

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NTB B 101
ChainResidue
BGLY48
BDIQ100
BHOH102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
AGLY78
BGLY78

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
AGLY78
BGLY78

218853

PDB entries from 2024-04-24

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