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3OXW

Crystal Structure of HIV-1 I50V, A71V Protease in Complex with the Protease Inhibitor Darunavir

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 Residues21
DetailsBINDING SITE FOR RESIDUE 017 B 200
ChainResidue
AASP25
BASP25
BGLY27
BALA28
BASP30
BVAL32
BGLY48
BGLY49
BVAL50
BPRO81
BILE84
AGLY27
BHOH113
BHOH115
AALA28
AASP29
AASP30
AGLY48
AGLY49
AVAL50
AVAL82

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 017 D 200
ChainResidue
CASP25
CGLY27
CASP29
CASP30
CGLY48
CGLY49
CVAL50
CVAL82
DASP25
DGLY27
DALA28
DASP30
DVAL32
DGLY48
DGLY49
DVAL50
DPRO81
DVAL82
DHOH104
DHOH114

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 100
ChainResidue
AARG14
AGLY17
AHOH103
BARG14
BILE15
BGLY16
BGLY17
BHOH128

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 100
ChainResidue
AMET36
AASN37
BPRO39
BGLY40

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 C 100
ChainResidue
CPRO39
CGLY40
DMET36
DASN37

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 101
ChainResidue
BGLY52
BPHE53
BHOH134
DTHR91
DGLN92

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 101
ChainResidue
ALYS7
AARG8
AHOH111

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT D 100
ChainResidue
DLYS20
DGLU21
DHOH113

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 102
ChainResidue
ATRP6
BASN88
BTHR91
BGLN92

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 101
ChainResidue
AGLN61
BGLN18
BLEU19
CLYS45
CMET46

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 101
ChainResidue
CGLY16
CGLY17
DARG14
DGLY16
DGLY17
DPRO63
DHOH126

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 102
ChainResidue
DTHR12
DARG14
DLEU19
DGLU65
DCYS67
DGLY68

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 102
ChainResidue
AASP29
AARG87
AASN88
BTRP6

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 103
ChainResidue
BGLU21
BGLU34
BVAL82
BASN83

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 102
ChainResidue
CARG8
CLEU10
CHOH106
CILE3

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 103
ChainResidue
BLYS41
BLYS43
BGLN58
BASP60
BHOH119

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 104
ChainResidue
CGLU21
CGLU34
CVAL82
CASN83

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 104
ChainResidue
AVAL50
AGLY51
BILE54
BPRO79

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

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PDB entries from 2024-07-24

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