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3QP0

HIV-1 protease (mutant Q7K L33I L63I) in complex with a novel inhibitor

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 Residues4
DetailsBINDING SITE FOR RESIDUE CL A 100
ChainResidue
ATHR74
AASN88
AHOH111
BARG41

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 100
ChainResidue
BTHR74
BASN88
BHOH232

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 101
ChainResidue
BTRP6

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NI8 B 102
ChainResidue
AGLY27
AASP29
AASP30
AVAL32
AGLY49
AILE50
AILE84
BASP25
BASP29
BASP30
BGLY49
BILE50
BHOH167
BHOH230
BHOH231
AASP25

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
AASP25
BASP25

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APHE99
BPHE99

222415

PDB entries from 2024-07-10

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