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4FCO

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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ATYR99
AGLN101
AGLN103
ALYS266
AHOH782
AHOH795

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AARG109
AHOH771

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
APRO71
ASER106
AHIS193
APRO195
AHOH645
AHOH819
AHOH961
ASER70

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE 0U4 A 504
ChainResidue
AGLY59
AGLN60
AGLY61
ALEU78
AASP80
AGLY82
ASER83
ATYR119
ATHR120
AGLN121
APHE156
ATRP163
ATYR246
AASP276
ASER277
AGLY278
ATHR279
ATHR280
AASN281
AARG283
ASER373
ATHR377
AALA383
AURE506
AHOH751

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE URE A 505
ChainResidue
AHOH672
AHOH681
AHOH699

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE URE A 506
ChainResidue
A0U4504
AHOH635
AHOH884

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE77-VAL88

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP80
AASP276

site_idSWS_FT_FI2
Number of Residues7
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241
ChainResidueDetails
ALYS113
ALYS262
ALYS266
ALYS272
ALYS286
ALYS287
ALYS294

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN140
AASN159
AASN210
AASN341

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PDB entries from 2024-11-06

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