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2QNQ

HIV-1 Protease in complex with a chloro decorated pyrrolidine-based 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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 2602
ChainResidue
ATHR74
AASN88
BARG41

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 2603
ChainResidue
BTHR74
BASN88
BHOH3063

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE QN3 A 2501
ChainResidue
AASP30
AGLY48
AILE50
AILE84
BASP25
BGLY27
BALA28
BGLY48
BGLY49
BILE50
BPRO81
BILE84
BHOH3049
AASP25
AGLY27
AALA28

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

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

221051

PDB entries from 2024-06-12

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