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2IEN

Crystal structure analysis of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017)

Replaces:  1S6G
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 Residues7
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AARG41
AASP60
AHOH1033
AHOH1098
AHOH1100
AHOH1145
AHOH1201

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 502
ChainResidue
BTRP106

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
AASN88
AHOH1191
BARG141
ATHR74

site_idAC4
Number of Residues29
DetailsBINDING SITE FOR RESIDUE 017 B 402
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH1233
BASP125
BGLY127
BALA128
BASP129
BASP130
BVAL132
BGLY148
BGLY149
BILE150
BPRO181
BVAL182
BILE184
BHOH1068
BHOH1222
BHOH1223
BHOH1224

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ACY B 601
ChainResidue
BPRO139
BGLY140
BARG141
BTYR159
BASP160
BHOH1053
BHOH1110
BHOH1187
BHOH1192
BHOH1210

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY A 602
ChainResidue
AGLN2
AHOH1063
AHOH1153
BGLU135

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 801
ChainResidue
BLYS155
BARG157
BHOH1052
BHOH1109
BHOH1113
BHOH1160

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 802
ChainResidue
AGLN18
AMET36
ASER37
BGLU165
BILE166
BALA167
BGLY168
BHOH1034
BHOH1083
BHOH1090
BHOH1136

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVI
ChainResidueDetails
AALA22-ILE33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029
ChainResidueDetails
ATHR26
BTHR126

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease
ChainResidueDetails
APRO1
BPRO101

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP25
BASP125

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE199

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BTHR126
BASP125

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP125

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PDB entries from 2024-07-10

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