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1N5R

Crystal structure of the mouse acetylcholinesterase-propidium complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001919biological_processregulation of receptor recycling
A0002076biological_processosteoblast development
A0003990molecular_functionacetylcholinesterase activity
A0004104molecular_functioncholinesterase activity
A0005515molecular_functionprotein binding
A0005518molecular_functioncollagen binding
A0005576cellular_componentextracellular region
A0005604cellular_componentbasement membrane
A0005615cellular_componentextracellular space
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006581biological_processacetylcholine catabolic process
A0007155biological_processcell adhesion
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0017171molecular_functionserine hydrolase activity
A0031594cellular_componentneuromuscular junction
A0031623biological_processreceptor internalization
A0042166molecular_functionacetylcholine binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043236molecular_functionlaminin binding
A0045202cellular_componentsynapse
A0048471cellular_componentperinuclear region of cytoplasm
A0052689molecular_functioncarboxylic ester hydrolase activity
A0060041biological_processretina development in camera-type eye
A0095500biological_processacetylcholine receptor signaling pathway
A0098552cellular_componentside of membrane
A0120162biological_processpositive regulation of cold-induced thermogenesis
B0001919biological_processregulation of receptor recycling
B0002076biological_processosteoblast development
B0003990molecular_functionacetylcholinesterase activity
B0004104molecular_functioncholinesterase activity
B0005515molecular_functionprotein binding
B0005518molecular_functioncollagen binding
B0005576cellular_componentextracellular region
B0005604cellular_componentbasement membrane
B0005615cellular_componentextracellular space
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0006581biological_processacetylcholine catabolic process
B0007155biological_processcell adhesion
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0017171molecular_functionserine hydrolase activity
B0031594cellular_componentneuromuscular junction
B0031623biological_processreceptor internalization
B0042166molecular_functionacetylcholine binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043236molecular_functionlaminin binding
B0045202cellular_componentsynapse
B0048471cellular_componentperinuclear region of cytoplasm
B0052689molecular_functioncarboxylic ester hydrolase activity
B0060041biological_processretina development in camera-type eye
B0095500biological_processacetylcholine receptor signaling pathway
B0098552cellular_componentside of membrane
B0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpmsVtLfGeSAG
ChainResidueDetails
APHE190-GLY205

site_idPS00941
Number of Residues11
DetailsCARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWtP
ChainResidueDetails
AGLU94-PRO104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
ASER203
BSER203

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AGLU334
AHIS447
BGLU334
BHIS447

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN265
BASN265

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN350
AASN464
BASN350
BASN464

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qe3
ChainResidueDetails
AGLU334
AHIS447
ASER203

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qe3
ChainResidueDetails
BGLU334
BHIS447
BSER203

227561

PDB entries from 2024-11-20

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