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3OXX

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

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 Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 100
ChainResidue
ATRP6
ALYS7
AARG8
BARG87

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 101
ChainResidue
CTRP6
AGLY40
BGLU35
BMET36
BASN37
CTHR4

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 102
ChainResidue
BHIS69
BLYS70
CPHE53
CHOH137

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT B 103
ChainResidue
BLYS20
BGLU21
BASN83

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT B 104
ChainResidue
BGLU35
CTHR4
CLEU5
CTRP6
DTHR91
DGLY94
DCYS95

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 105
ChainResidue
BGLY73
BTHR74
BASN88
BHOH133

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE DR7 A 100
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AGLY48
AGLY49
AILE84
AHOH103
BARG8
BASP25
BGLY27
BALA28
BASP29
BGLY48
BGLY49
BVAL82
BILE84

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 101
ChainResidue
AASP29
AARG87
AASN88
AEDO102
AHOH136
BTRP6

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 102
ChainResidue
AARG87
AGOL101
BLYS7
BARG8

site_idBC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE DR7 C 100
ChainResidue
CARG8
CASP25
CGLY27
CALA28
CASP29
CGLY48
CGLY49
CILE84
CHOH105
DARG8
DASP25
DGLY27
DALA28
DASP29
DGLY48
DGLY49
DVAL50
DPRO81
DILE84

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C 101
ChainResidue
ATRP42
APRO44
CLEU10
CVAL11
CTHR12
CCYS67
CACT104

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 102
ChainResidue
ATRP6
BGLY94
BHOH115
CVAL50
CGLY51
CHOH134
DPRO79
DPRO81

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT C 103
ChainResidue
CLYS7
CARG8
DARG87
DGOL100

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT C 104
ChainResidue
ATRP42
CGOL101

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 100
ChainResidue
DARG87
DASN88
CTRP6
CACT103
DASP29

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 D 101
ChainResidue
CPRO39
CGLY40
DMET36
DASN37

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT D 102
ChainResidue
DGLY73
DTHR74
DASN88
DGLN92

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO D 103
ChainResidue
CARG87
DLYS7
DARG8

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
CASP25
DASP25

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

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PDB entries from 2024-10-30

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