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

4R95

BACE-1 in complex with 2-(((1R,3S)-3-(((R)-4-(2-cyclohexylethyl)-2-iminio-1-methyl-5-oxoimidazolidin-4-yl)methyl)cyclohexyl)amino)quinolin-1-ium

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
A0016020cellular_componentmembrane
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TLA A 501
ChainResidue
ALYS300
AHOH750
AHOH829
AHOH896
BHIS106
BPRO107
BPHE108
BASP167
BLYS168

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TLA A 502
ChainResidue
AARG68
AASN89
AHIS110
AARG111
AASN175
AHOH712
AHOH816
AHOH840

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 3KW A 503
ChainResidue
AASP93
AGLY95
AVAL130
ATYR132
AGLN134
ALYS168
APHE169
AILE171
AARG189
AASP289
AGLY291
ATHR292
AHOH933
AHOH934

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TLA B 501
ChainResidue
BARG68
BASN89
BHIS110
BARG111
BASN175
BHOH785
BHOH786
BHOH804
BHOH944

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 3KW B 502
ChainResidue
BASP93
BGLY95
BTYR132
BLYS168
BPHE169
BILE171
BARG189
BASP289
BGLY291
BTHR292

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ILVDTGSSNFAV
ChainResidueDetails
AILE90-VAL101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
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 Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon