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4Q1Y

Mutations Outside the Active Site of HIV-1 Protease Alter Enzyme Structure and Dynamic Ensemble of the Active Site to Confer Drug Resistance

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 PO4 A 101
ChainResidue
AARG14
AGLY16
AGLY17
AHOH229
AHOH259
BARG14
BGLY16
BHOH203
BHOH207

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 102
ChainResidue
ATRP6
AGLY49
APHE53
BPRO81
BGLN92

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 103
ChainResidue
ALYS7
AARG8
AHOH243

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 104
ChainResidue
AARG14
ALEU19
APRO44
ALYS45

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 105
ChainResidue
ALYS70
BPRO1

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 017 A 106
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AILE50
AHOH202
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BHOH245

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 101
ChainResidue
BGLY73
BTHR74
BASN88

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTIF
ChainResidueDetails
AALA22-PHE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000305|PubMed:33542150
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 175
ChainResidueDetails
AASP25hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ATHR26electrostatic stabiliser, transition state stabiliser
AGLY27electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 175
ChainResidueDetails
BASP25hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BTHR26electrostatic stabiliser, transition state stabiliser
BGLY27electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-04-24

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