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3VF5

Crystal Structure of HIV-1 Protease Mutant I47V with novel P1'-Ligands GRL-02031

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 Residues6
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AASP60
AHOH606
AHOH616
AHOH656
AHOH665
AHOH666

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 502
ChainResidue
ATHR74
AASN88
BARG41

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AVAL47
AGLY48
B031201

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 504
ChainResidue
AGLY40
AARG41
ATRP42

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 505
ChainResidue
ATRP42
ALYS55
AVAL56
AARG57
AHOH674

site_idAC6
Number of Residues33
DetailsBINDING SITE FOR RESIDUE 031 B 201
ChainResidue
AARG8
ALEU23
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL47
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
ACL503
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL47
BGLY48
BGLY49
BILE50
BPRO81
BVAL82
BILE84
BHOH1001
BHOH1002
BHOH1097
BHOH1098
BHOH1100

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 202
ChainResidue
BASP60
BHOH1064
BHOH1065
BHOH1090

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 203
ChainResidue
BTHR74
BASN88
BHOH1013

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 204
ChainResidue
BTRP6

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 205
ChainResidue
ATHR4
ALEU5
ATRP6
BTHR91
BALA95
BTHR96

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

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
ChainResidueDetails
AASP25
BASP25

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

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PDB entries from 2024-07-24

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