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2IDW

Crystal structure analysis of HIV-1 protease mutant V82A with a potent non-peptide inhibitor (UIC-94017)

Replaces:  1S65
Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0042802molecular_functionidentical protein binding
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
AGLY73
ATHR74
AASN88
AHOH1163
AHOH1237

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PO4 A 701
ChainResidue
AHOH1013
AHOH1057
AHOH1063
AHOH1247
AHOH1262
BLYS114
BGLY117
BACY606
BHOH1154
ALYS14
AILE15
AGLY16
AGLY17

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 702
ChainResidue
APRO39
AGLY40
AHOH1115
AHOH1270
BMET136
BSER137

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 703
ChainResidue
BPRO101
BARG157
BHIS169
BHOH1049
BHOH1133
BHOH1210

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 704
ChainResidue
ALYS20
AGLU21
AGLU34
AARG41
AASN83
AHOH1136
AHOH1164
AHOH1266

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 017 B 401
ChainResidue
AASP25
AGLY27
AALA28
AASP30
AVAL32
AILE47
AGLY48
AGLY49
APRO81
AILE84
BASP125
BGLY127
BALA128
BASP129
BASP130
BGLY148
BGLY149
BILE150
BHOH1001
BHOH1138

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE DMS A 901
ChainResidue
APRO1
ALYS55
AACY605
AHOH1248
BGLY168
BHIS169
BLYS170
BHOH1121
BHOH1225

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 601
ChainResidue
AMET36
ASER37
BPRO139

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY B 602
ChainResidue
AGLN92
BGLY149
BHOH1214

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY B 603
ChainResidue
ATRP6
BTHR191
BGLY194
BHOH1025
BHOH1205
BHOH1230

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY B 604
ChainResidue
BLEU110
BVAL111
BTHR112
BGLU121

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACY A 605
ChainResidue
AMET46
APHE53
ALYS55
ADMS901
AHOH1012
BHOH1121
BHOH1225

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY B 606
ChainResidue
ALYS14
ALYS70
APO4701
AHOH1247
BLYS114
BLYS155
BGLU165
BHOH1154

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 801
ChainResidue
APRO44
AVAL56
AHOH1032
AHOH1058
BHOH1052
ATRP42

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

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

219140

PDB entries from 2024-05-01

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