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3KYR

Bace-1 in complex with a norstatine type inhibitor

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 Residues17
DetailsBINDING SITE FOR RESIDUE 038 A 500
ChainResidue
AGLY34
AARG128
ATYR198
ALYS224
AILE226
AASP228
AARG235
ATHR329
AHOH401
ASER35
ATYR68
AVAL69
APRO70
ATYR71
ATHR72
ALYS75
AILE126

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 038 B 500
ChainResidue
AASP4
BGLY34
BTYR68
BVAL69
BPRO70
BTYR71
BTHR72
BARG128
BTYR198
BASP228
BARG235
BTHR329

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 038 C 500
ChainResidue
CGLY34
CTYR68
CVAL69
CPRO70
CTYR71
CTHR72
CARG128
CTYR198
CLYS224
CASP228
CTHR231
CARG235

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

245011

PDB entries from 2025-11-19

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