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2HS1

Ultra-high resolution X-ray crystal structure of HIV-1 protease V32I mutant with TMC114 (darunavir) inhibitor

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 Residues4
DetailsBINDING SITE FOR RESIDUE CL A 901
ChainResidue
AVAL11
ATHR12
AHOH1253
BLYS107

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 902
ChainResidue
ALYS7
BVAL111
BTHR112
BHOH1056

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 903
ChainResidue
AGLY40
BLYS155
ALEU38

site_idAC4
Number of Residues29
DetailsBINDING SITE FOR RESIDUE 017 A 201
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
APRO81
AVAL82
AILE84
AHOH1001
AHOH1005
AHOH1006
AHOH1224
BARG108
BASP125
BGLY127
BALA128
BASP129
BASP130
BILE132
BGLY148
BGLY149
BILE150
BPRO181
BVAL182
BHOH1002

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 017 B 203
ChainResidue
ATRP6
AGLY40
AARG41
BGLU135
BPRO144
BLYS145
BLYS155
BVAL156
BARG157
BGLY168
BVAL177
BGLY178
BGLN192
BGLY194
BHOH1023
BHOH1051
BHOH1074
BHOH1086
BHOH1098
BHOH1143
BHOH1254

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS B 204
ChainResidue
ATRP6
BTRP142
BARG157
BHOH1023
BHOH1074

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTII
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

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PDB entries from 2024-10-30

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