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3UDP

Crystal Structure of BACE with Compound 12

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 09D A 501
ChainResidue
ALEU30
ATYR198
AASP228
AGLY230
AHOH702
AHOH821
AASP32
AGLY34
ATYR71
ATHR72
AGLN73
APHE108
AILE126
AARG128

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 502
ChainResidue
AARG96
AASN98
AGLU134
AHOH715

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
ATYR222
ATYR384
AHOH767
AHOH861

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PEG A 504
ChainResidue
AGLY11
AGLN12
AGLY13
ASER229
AGLY230
ATHR231
ATHR232
AALA335
AHOH760

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 505
ChainResidue
AASP131
AHIS397
AHOH822
AHOH898

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 506
ChainResidue
AGLU255
ATRP270
AASP390
AHIS396
AHIS398

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

223532

PDB entries from 2024-08-07

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