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4OBH

Crystal Structure of Inactive HIV-1 Protease in Complex with the p1-p6 substrate variant (L449F)

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 Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 101
ChainResidue
AARG14
AGLY16
AGLY17
APRO63
AHOH210
AHOH257
AHOH262

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 102
ChainResidue
AHOH235
BARG87
ALYS7
AARG8

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 103
ChainResidue
ATRP6
AHOH219
AHOH239
BARG87
BASN88

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 104
ChainResidue
AARG14

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 105
ChainResidue
APRO39
AGLY40
BLYS20
BMET36
BASN37

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 106
ChainResidue
APRO81
EARG1
EPRO2

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 107
ChainResidue
ATHR12
AGLU65
ACYS67
AGLY68

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 101
ChainResidue
AGLN18
AMET36
AASN37
BPRO39
BGLY40

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 102
ChainResidue
AASN88
ATHR91
BTRP6

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT C 101
ChainResidue
CMET36
CASN37
DPRO39
DGLY40

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 102
ChainResidue
CASP29
CASP30
FARG1
FHOH102

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 103
ChainResidue
CTHR12
CGLU65
CCYS67
CGLY68

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 104
ChainResidue
CLYS20
CGLU21
CGLU34
CASN83
CHOH228

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL D 101
ChainResidue
CARG87
DLYS7
DARG8

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 102
ChainResidue
CTRP6
DASP29
DARG87
DPO4107
FARG9
FHOH103

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D 103
ChainResidue
DGLY73
DTHR74
DASN88
DGLN92
DHOH231

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO D 105
ChainResidue
DGLU65
DCYS67
DGLY68

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO D 106
ChainResidue
CPRO63
DGLY16
DGLY17
DGLN18

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 D 107
ChainResidue
CLYS7
CARG8
DARG87
DGOL102
FARG9

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL E 101
ChainResidue
AARG87
BTRP6
BLYS7
BARG8
EARG9

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
EPHE5
FPHE5
CASN25
DASN25

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

224931

PDB entries from 2024-09-11

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