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4OBK

Crystal structure of inactive HIV-1 protease in complex with the P1-P6 substrate variant (L449F/S451N)

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 Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 101
ChainResidue
AARG14
AGLY16
AGLY17
AILE64
AGLU65
AHOH218
AHOH231
AHOH258
BGLY16

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 102
ChainResidue
ALYS7
AARG8
BARG87
CARG1

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 103
ChainResidue
AHIS69
ALYS70
BPRO1

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 101
ChainResidue
AARG87
BLYS7
BARG8
BHOH241
CARG9

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 102
ChainResidue
BLYS20
BGLU21
BGLU34
BASN83

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues138
DetailsDomain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Cleavage; by viral protease","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

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