Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6E3Z

Structure of Bace-1 in complex with Ligand 8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
C0004190molecular_functionaspartic-type endopeptidase activity
C0006508biological_processproteolysis
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue HRV A 401
ChainResidue
AGLY11
AASP228
ASER229
AGLY230
ATHR232
AALA335
AHOH589
AGLN12
AGLY13
ALEU30
AASP32
AGLY34
ATYR71
APHE108
AILE110

site_idAC2
Number of Residues14
Detailsbinding site for residue HRV B 401
ChainResidue
BGLY11
BGLN12
BGLY13
BLEU30
BASP32
BTYR71
BPHE108
BASP228
BSER229
BGLY230
BTHR231
BTHR232
BALA335
BHOH605

site_idAC3
Number of Residues13
Detailsbinding site for residue HRV C 401
ChainResidue
CGLY11
CGLN12
CGLY13
CLEU30
CASP32
CTYR71
CPHE108
CASP228
CSER229
CGLY230
CTHR232
CALA335
CHOH514

site_idAC4
Number of Residues13
Detailsbinding site for residue HRV C 402
ChainResidue
ALYS65
APRO129
AASP130
ASER132
CTHR-4
CGLY-3
CSER-2
CTYR68
CTRP76
CGLU77
CSER105
CHOH602
CHOH614

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 Residues6
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17425515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19011241","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon