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2O4N

Crystal Structure of HIV-1 Protease (TRM Mutant) 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 Residues22
DetailsBINDING SITE FOR RESIDUE TPV A 300
ChainResidue
AASP25
AILE50
APRO81
ALEU82
AHOH387
BARG8
BASP25
BGLY27
BALA28
BGLY48
BGLY49
AGLY27
BILE50
BLEU82
BGOL301
AALA28
AASP29
AASP30
AILE32
AILE47
AGLY48
AGLY49

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 301
ChainResidue
ATPV300
BALA28
BASP29
BILE47
BGLY48
BHOH332
BHOH333
BHOH348

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTIF
ChainResidueDetails
AALA22-PHE33

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

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PDB entries from 2024-06-12

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