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2O4P

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

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 Residues20
DetailsBINDING SITE FOR RESIDUE TPV A 300
ChainResidue
AARG8
AGLY49
AILE50
AHOH310
BARG8
BLEU23
BASP25
BGLY27
BGLY49
BILE50
BVAL82
ALEU23
BGOL301
AASP25
AGLY27
AALA28
AASP29
AASP30
AILE47
AGLY48

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
ATPV300
BALA28
BASP29
BGLY48
BHOH334
BHOH356

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 2024-10-16

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