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4Q1W

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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 101
ChainResidue
AARG14
AGLY16
AGLY17
AHOH247
BGLY16
BHOH208
BHOH221
BHOH233

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 102
ChainResidue
AGLU21
AHOH239
BHOH230
ALYS20

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 103
ChainResidue
AMET36
AASN37
AHOH249
BPRO39
BGLY40

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 017 A 104
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
AHOH206
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BPRO81
BVAL82
BHOH239

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 101
ChainResidue
AARG87
BTRP6
BLYS7
BARG8
BHOH232

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 102
ChainResidue
AGLY49
AHOH220
BTHR91
BGLN92
BHOH255

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

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 2024-07-31

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