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4KE1

Crystal structure of BACE1 in complex with hydroxyethylamine-macrocyclic inhibitor 19

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 401
ChainResidue
ASER105

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 402
ChainResidue
ALYS107
AHOH699

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 403
ChainResidue
AARG349

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 1R6 A 404
ChainResidue
APRO70
ATYR71
ATHR72
APHE108
AILE118
ATYR198
ALYS224
AASP228
AGLY230
ATHR232
ATHR329
AGLN12
ALEU30
AASP32
AGLY34
ASER35

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 405
ChainResidue
AARG50
ATYR51
AGLN53
ASER187
AHOH594
AHOH639
AHOH698

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE29-VAL40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP32
AASP228

site_idSWS_FT_FI2
Number of Residues7
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS65
ALYS214
ALYS218
ALYS224
ALYS238
ALYS239
ALYS246

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN92
AASN111
AASN162
AASN293

218853

PDB entries from 2024-04-24

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