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2Q3K

Crystal Structure of Lysine Sulfonamide Inhibitor Reveals the Displacement of the Conserved Flap Water Molecule in HIV-1 Protease

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 Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
AGLY16
AHOH518
BGLY16
BGLY17
BHOH514
BHOH522
BHOH564

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 503
ChainResidue
BGLY68
BHIS69
BLYS70
BHOH536
APRO1
AHOH526

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 504
ChainResidue
BTHR91
BHOH510

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 505
ChainResidue
ALYS20
AGLU21
AGLU34
AASN83

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 506
ChainResidue
ALYS7
AARG8
AHOH539

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE MUW A 200
ChainResidue
AASP25
AGLY27
AALA28
AASP29
AILE47
AGLY48
AGLY49
AILE50
AVAL82
AILE84
AHOH517
BARG8
BASP25
BALA28
BASP30
BGLY48
BGLY49
BILE50
BPRO81
BILE84
BHOH530

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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