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5E5J

Joint X-ray/neutron structure of HIV-1 protease triple mutant (V32I,I47V,V82I) with darunavir 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
A0055036cellular_componentvirion membrane
A0072494cellular_componenthost multivesicular body
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0042802molecular_functionidentical protein binding
B0055036cellular_componentvirion membrane
B0072494cellular_componenthost multivesicular body
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue 017 A 201
ChainResidue
AASP25
AILE84
ADOD312
BASP25
BGLY27
BALA28
BASP30
BILE32
BVAL47
BGLY48
BGLY49
AGLY27
BILE82
BDOD253
AASP29
AASP30
AILE32
AVAL47
AGLY48
AILE50
AILE82

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

247536

PDB entries from 2026-01-14

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