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3OXV

Crystal Structure of HIV-1 I50V, A71 Protease in Complex with the protease inhibitor amprenavir.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
D0004190molecular_functionaspartic-type endopeptidase activity
D0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 478 B 200
ChainResidue
AASP25
AILE84
BASP25
BGLY27
BALA28
BASP30
BGLY48
BGLY49
BPRO81
BVAL82
BILE84
AGLY27
BHOH105
AALA28
AASP29
AASP30
AGLY48
AGLY49
AVAL50
AVAL82

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 100
ChainResidue
APRO39
AGLY40
BMET36
BASN37
BHOH114

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 101
ChainResidue
BPHE53
BHOH122
BHOH127

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 478 A 200
ChainResidue
AGLU35
ATRP42
ALYS55
AVAL56
AARG57
AVAL77
DTHR12
DCYS67
DGLY68

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT D 100
ChainResidue
ALYS41
ATRP42

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 D 101
ChainResidue
CARG14

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 102
ChainResidue
DGLU21
DGLU34
DPRO81
DVAL82
DASN83

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT D 103
ChainResidue
CPRO39
CGLY40
DMET36
DASN37

site_idAC9
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 478 C 200
ChainResidue
CASP25
CGLY27
CALA28
CASP29
CASP30
CVAL32
CGLY48
CGLY49
CVAL50
CILE84
CHOH119
DASP25
DGLY27
DALA28
DASP30
DVAL32
DGLY48
DGLY49
DPRO81
DVAL82
DILE84

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 C 100
ChainResidue
CMET36
CASN37
CHOH164
DPRO39
DGLY40
DHOH151

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
BALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
BASP25
AASP25
DASP25
CASP25

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
BPHE99
APHE99
DPHE99
CPHE99

221051

PDB entries from 2024-06-12

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