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2ZDZ

X-ray structure of Bace-1 in complex with compound 3.b.10

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 310 A 1
ChainResidue
AGLY73
AILE172
ATRP177
AILE180
AASP290
ASER291
AGLY292
ATHR294
AHOH502
AHOH611
AGLN74
AGLY75
ALEU92
AASP94
AGLY96
ATYR133
ATRP138
APHE170

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE91-VAL102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP94
AASP290

site_idSWS_FT_FI2
Number of Residues7
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS127
ALYS276
ALYS280
ALYS286
ALYS300
ALYS301
ALYS308

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN154
AASN173
AASN224
AASN355

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PDB entries from 2024-04-24

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