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2NNK

Crystal structure analysis of HIV-1 protease mutant I84V with a inhibitor saquinavir

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AASP60
AHOH1060
AHOH1064
AHOH1068
AHOH1127
AHOH1132

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 502
ChainResidue
BHOH1135
BHOH1190
BASP160
BHOH1080
BHOH1112

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
ATHR74
AASN88
AHOH1147
AHOH1159
BARG141

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 504
ChainResidue
BTRP106

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 505
ChainResidue
BTHR174
BASN188
BHOH1023

site_idAC6
Number of Residues28
DetailsBINDING SITE FOR RESIDUE ROC A 401
ChainResidue
AARG8
AASP25
AGLY27
AALA28
AASP29
AASP30
AGLY48
AGLY49
AILE50
ATHR80
APRO81
AHOH1002
AHOH1011
AHOH1032
BARG108
BLEU123
BASP125
BGLY127
BASP129
BASP130
BILE147
BGLY148
BGLY149
BILE150
BTHR180
BPRO181
BVAL184
BHOH1001

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 601
ChainResidue
ALYS7
AARG8
AHOH1160

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 603
ChainResidue
AARG87
AHOH1020
AHOH1048
AHOH1184
BTRP106
BARG108

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 604
ChainResidue
AGLY94
BTRP142
BLYS155
BVAL156
BARG157

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
ChainResidueDetails
ATHR26
BTHR126

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APRO1
BPRO101

218853

PDB entries from 2024-04-24

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