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4EQJ

Crystal Structure of inactive single chain variant of HIV-1 Protease in Complex with the substrate RT-RH

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 EDO A 201
ChainResidue
ALYS41
ALYS43
AGLN58
AASP60

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 202
ChainResidue
ATHR91
ATHR96
ATRP106
AHOH367

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 203
ChainResidue
ALYS107
AARG108
AHOH365
AARG87

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 204
ChainResidue
AARG114
AGLY117
AGLU165
AGOL207

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 205
ChainResidue
ATHR91
AGLN92
AGLY151
AGLY152
APHE153

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 206
ChainResidue
ATRP6
AILE50
AGLY51
AGLY100
APRO181
AGLN192
AGLY194

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 207
ChainResidue
AARG14
AGLY16
AGLY17
AILE115
AGLY117
APRO163
AEDO204

site_idAC8
Number of Residues25
DetailsBINDING SITE FOR CHAIN G OF SUBSTRATE RT-RH
ChainResidue
AARG8
ALEU23
AASN25
AGLY27
ASER28
AASP29
APHE30
AARG48
APRO81
AVAL82
AILE84
AARG108
AASN125
AGLY127
ASER128
AASP129
AVAL132
AILE147
AGLY148
AGLY149
AILE150
AVAL182
AILE184
GHOH101
GHOH102

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

224931

PDB entries from 2024-09-11

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