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5E5K

Joint X-ray/neutron structure of HIV-1 protease triple mutant (V32I,I47V,V82I) with darunavir at pH 4.3

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 Residues21
Detailsbinding site for residue 017 B 201
ChainResidue
AASP25
BASP25
BGLY27
BALA28
BASP30
BILE32
BGLY48
BGLY49
BPRO81
BILE82
BDOD307
AGLY27
BDOD315
BDOD326
AASP29
AASP30
AILE32
AVAL47
AGLY48
AILE50
AILE84

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues138
DetailsDomain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsRegion: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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