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2O4L

Crystal Structure of HIV-1 Protease (Q7K, I50V) in Complex with Tipranavir

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0044174cellular_componenthost cell endosome
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0044174cellular_componenthost cell endosome
B0055036cellular_componentvirion membrane
B0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
ATHR74
AASN88
AHOH461
BARG41

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 402
ChainResidue
BTHR74
BASN88
BHOH413
BHOH490
BHOH530

site_idAC3
Number of Residues39
DetailsBINDING SITE FOR RESIDUE TPV A 403
ChainResidue
AARG8
ALEU23
AASP25
AGLY27
AALA28
AASP29
AASP30
AVAL32
AILE47
AGLY48
AGLY49
AVAL50
APRO81
AVAL82
AILE84
AGOL405
AHOH428
AHOH588
AHOH589
AHOH590
BARG8
BLEU23
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BILE47
BGLY48
BGLY49
BVAL50
BPRO81
BVAL82
BGOL404
BHOH420
BHOH448
BHOH535
BHOH597

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 404
ChainResidue
ATPV403
BALA28
BASP29
BILE47
BGLY48
BHOH443
BHOH535
BHOH597

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
AALA28
AASP29
AGLY48
ATPV403
AHOH474
AHOH588
AHOH590

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
ATHR26
BTHR26

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
APRO1
BPRO1

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

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PDB entries from 2025-06-18

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