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3UQU

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 Residues23
DetailsBINDING SITE FOR RESIDUE ZPX A 394
ChainResidue
AGLY11
AGLN73
APHE108
ATRP115
AASP228
ASER229
AGLY230
ATHR231
ATHR232
AASN233
AARG235
AGLN12
AARG307
ASER325
AALA335
AHOH633
AGLY13
ATYR14
ALEU30
AASP32
AGLY34
ATYR71
ATHR72

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 395
ChainResidue
ATHR72
AARG235
ASER327
ASER328
ATHR329

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 396
ChainResidue
ATYR51
AGLN53
AGLN55
ALYS218
AHOH630

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 397
ChainResidue
APRO70
AARG351
AHOH548
AHOH671
AHOH697

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE URE A 398
ChainResidue
AARG61
AASP62
AHOH480
AHOH621

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 399
ChainResidue
AGLY186

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE URE A 400
ChainResidue
AASP62
ALEU213
AMET215
AHOH543

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 2024-09-11

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