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5T8H

Joint X-ray/neutron structure of HIV-1 protease triple mutant (V32I,I47V,V82I) with amprenavir at pH 6.0

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0042802molecular_functionidentical protein binding
A0044174cellular_componenthost cell endosome
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0042802molecular_functionidentical protein binding
B0044174cellular_componenthost cell endosome
B0055036cellular_componentvirion membrane
B0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue 478 B 401
ChainResidue
AASP25
BGLY127
BALA128
BASP130
BILE132
BVAL147
BGLY148
BGLY149
BILE150
BILE182
BDOD509
AGLY27
BDOD516
AASP29
AASP30
AILE32
AGLY48
AGLY49
AILE50
BASP125

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTII
ChainResidueDetails
AALA22-ILE33

237423

PDB entries from 2025-06-11

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