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4FRK

Crystal structure of BACE1 in complex with aminooxazoline xanthene 11a

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 401
ChainResidue
ASER105

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 402
ChainResidue
ALYS107
AHOH512

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 403
ChainResidue
ATYR222
AHOH565

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 404
ChainResidue
AARG349
AHOH754

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE DWD A 405
ChainResidue
AGLY13
ALEU30
AASP32
ATYR71
APHE108
ATYR198
AASP228
AGLY230
AGLU265
AHOH644
AHOH779
AGLY11
AGLN12

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 406
ChainResidue
AARG50
ATYR51
AGLN53
ASER187
AHOH739

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 407
ChainResidue
ASER10
AGLY11
AGLN12
AGLY13
ATYR14
AVAL170
AALA335
AGLU339
AHOH536
AHOH646
AHOH647

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

220472

PDB entries from 2024-05-29

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