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4EP3

Crystal Structure of inactive single chain wild-type HIV-1 Protease in Complex with the substrate CA-p2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
AARG14
AGLY17
APRO63
AGLU65
AGLY117
AHOH340

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
APRO139
AGLY140
ALYS20
AMET36
AASN37

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 203
ChainResidue
ATRP6
AASP129
AARG187
AASN188

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 204
ChainResidue
AARG87
ALYS107
AARG108

site_idAC5
Number of Residues27
DetailsBINDING SITE FOR CHAIN E OF SUBSTRATE CA-P2
ChainResidue
AARG8
AASN25
AGLY27
AALA28
AASP29
AASP30
AMET46
AILE47
AGLY48
AGLY49
AILE50
ALEU76
AVAL82
AILE84
AARG108
AASN125
AGLY127
AALA128
AASP129
AASP130
AGLY148
AGLY149
AILE150
AILE184
AHOH323
EHOH101
EHOH102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASN125

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE199

223532

PDB entries from 2024-08-07

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