Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3QAA

HIV-1 wild type protease with a substituted bis-Tetrahydrofuran inhibitor, GRL-044-10A

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 Residues30
DetailsBINDING SITE FOR RESIDUE G04 A 401
ChainResidue
AASP25
AILE50
APRO81
AVAL82
AILE84
AHOH1002
AHOH1095
AHOH1096
AHOH1105
BARG108
BASP125
AGLY27
BGLY127
BALA128
BASP129
BASP130
BGLY148
BGLY149
BILE150
BPRO181
BVAL182
BILE184
AALA28
BHOH1001
AASP29
AASP30
AVAL32
AILE47
AGLY48
AGLY49

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AASP60
AHOH1057
AHOH1058
AHOH1059
AHOH1060
AHOH1093

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 511
ChainResidue
ATHR74
AASN88
BARG141

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 512
ChainResidue
BTRP106

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 521
ChainResidue
AGLN18
AMET36
ASER37
AHOH1027
BTHR112
BGLU165
BALA167
BGLY168

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 522
ChainResidue
ALYS45
AMET46
BGLN161
BHOH1023
BHOH1031

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 523
ChainResidue
BLYS155
BARG157
BVAL177
BGLY178
BHOH1120

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
AASP25
BASP125

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069
ChainResidueDetails
APHE99
BPHE199

226262

PDB entries from 2024-10-16

PDB statisticsPDBj update infoContact PDBjnumon