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3UDM

Crystal Structure of BACE with Compound 8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 09A A 501
ChainResidue
ALEU30
AGLY230
AHOH813
AASP32
AGLY34
ATYR71
AGLN73
APHE108
AILE126
ATYR198
AASP228

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AGLU255
AASP390
AHIS396
AHIS398

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PEG A 504
ChainResidue
AGLY11
AGLN12
AGLY13
AILE110
ASER229
AGLY230
ATHR231
ATHR232
AALA335
AHOH712

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

226707

PDB entries from 2024-10-30

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