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3VF7

Crystal Structure of HIV-1 Protease Mutant L76V 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 Residues25
DetailsBINDING SITE FOR RESIDUE 031 A 201
ChainResidue
ALEU23
APRO81
AVAL82
AILE84
AHOH1001
AHOH1069
BASP25
BGLY27
BALA28
BASP30
BVAL32
AASP25
BGLY48
BGLY49
BPRO81
BVAL82
BILE84
BGOL503
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 202
ChainResidue
AHOH1016
AHOH1041
AHOH1063
AHOH1071
AHOH1076
AHOH1105

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 203
ChainResidue
ATRP6
ALYS55
AGOL206

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 204
ChainResidue
ATHR74
AASN88
AHOH1015

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 205
ChainResidue
AGLN61
AGLN92
AHOH1006
AHOH1007
AHOH1068
BLYS45
BMET46
BPHE53

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 206
ChainResidue
ATHR4
ATRP6
APRO44
ALYS55
ACL203
AHOH1042
AHOH1046

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 207
ChainResidue
ATHR12
AGLU65
AILE66
AALA67
AGLY68
AHOH1037
AHOH1084
BGLN18
BMET36
BSER37

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 208
ChainResidue
AGLY40
AHOH1025
AHOH1071
BLYS70
BALA71

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 501
ChainResidue
BASP60
BHOH630
BHOH631
BHOH632
BHOH634
BHOH674

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 502
ChainResidue
AARG41
BTHR74
BASN88

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 503
ChainResidue
A031201
AHOH1039
BARG8
BVAL82

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 2024-11-06

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