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4BFD

CRYSTAL STRUCTURE OF BACE-1 IN COMPLEX WITH CHEMICAL LIGAND

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 8T3 A 1447
ChainResidue
AGLY72
AGLY291
ATHR292
ATHR293
AALA396
AHOH2021
AHOH2315
AGLY74
ALEU91
AASP93
ATYR132
APHE169
AILE171
AASP289
ASER290

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1448
ChainResidue
AHIS242
ATYR245
AHOH2192
AHOH2193
AHOH2196
AHOH2316

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1449
ChainResidue
AVAL202
ATHR205
AHOH2168
AHOH2169
AHOH2171

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 1450
ChainResidue
AARG157
AASN159

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE90-VAL101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP93
AASP289

site_idSWS_FT_FI2
Number of Residues7
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS126
ALYS275
ALYS279
ALYS285
ALYS299
ALYS300
AALA307

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN153
AASN172
AASN223
AASN354

229183

PDB entries from 2024-12-18

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