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4IVT

Crystal structure of BACE1 with its inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE VTI A 401
ChainResidue
AASP32
AGLY230
ATHR231
AARG235
AHOH911
AHOH912
ATYR71
ATHR72
AGLN73
ALYS107
APHE108
AILE110
ATRP115
AASP228

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
ATYR51
AGLN53
AGLN55
ALYS218
AHOH657
AHOH712

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ASER22
APRO23
ASER58
AHIS145
APRO147
AHOH560
AHOH675

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

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PDB entries from 2024-06-26

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