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4EPJ

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
ATRP6
AASP129
AARG187
AASN188

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 202
ChainResidue
AGLY73
ATHR74
AASN88
AHOH318

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS A 203
ChainResidue
AARG8
AHOH360
ALYS7

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 204
ChainResidue
AASP29
AARG87
AASN88
ATRP106
AHOH344

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 205
ChainResidue
ALYS120
AGLU121

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 206
ChainResidue
ALYS107
AARG108
AHOH352

site_idAC7
Number of Residues23
DetailsBINDING SITE FOR CHAIN D OF SUBSTRATE P2-NC
ChainResidue
AASN25
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48
AGLY49
AILE50
ATHR80
AVAL82
AILE84
AASN125
AGLY127
AALA128
AASP129
AASP130
AILE147
AGLY148
AGLY149
AILE150
AHOH317
DHOH101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues69
DetailsDomain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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