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

5QDA

Crystal structure of BACE complex with BMC013

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 Residues19
Detailsbinding site for residue E74 A 401
ChainResidue
AGLN12
AGLN73
APHE108
ATRP115
AASP228
AGLY230
ATHR231
ATHR232
AARG235
AHOH503
AHOH564
ALEU30
AASP32
AGLY34
ASER35
AVAL69
APRO70
ATYR71
ATHR72

site_idAC2
Number of Residues17
Detailsbinding site for residue E74 B 401
ChainResidue
BLEU30
BASP32
BGLY34
BSER35
BPRO70
BTYR71
BTHR72
BPHE108
BTRP115
BTYR198
BASP228
BGLY230
BTHR231
BTHR232
BARG235
BHOH545
BHOH550

site_idAC3
Number of Residues19
Detailsbinding site for residue E74 C 401
ChainResidue
CGLN12
CLEU30
CASP32
CGLY34
CSER35
CVAL69
CPRO70
CTYR71
CTHR72
CGLN73
CTYR198
CASP228
CGLY230
CTHR231
CTHR232
CARG235
CHOH505
CHOH591
CHOH594

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

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon