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5T2Z

Crystal Structure of Multi-drug Resistant HIV-1 Protease PR-S17 in Complex with Darunavir

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 Residues24
Detailsbinding site for residue 017 B 201
ChainResidue
AASP25
AILE84
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL48
BGLY49
BILE50
BPRO81
AGLY27
BILE84
BHOH301
BHOH302
BHOH303
BHOH304
AALA28
AASP29
AASP30
AVAL48
AGLY49
AILE50
ASER82

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

237992

PDB entries from 2025-06-25

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