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3RTM

Structure of Bace-1 (Beta-Secretase) in Complex with 3-(2-Aminoquinolin-3-yl)-N-cyclohexyl-N-methylpropanamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 1502
ChainResidue
ASER105

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 1503
ChainResidue
ALYS107

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 1505
ChainResidue
AARG349

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 393
ChainResidue
AARG50
ATYR51
AGLN53

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 394
ChainResidue
AVAL170
ATHR232
AARG307
AGLU339
ALYS9
AGLY11
AGLY13

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE RTM A 395
ChainResidue
AASP32
ASER35
AILE118
AASP228
AGLY230
ATHR231

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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