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1P0I

Crystal structure of human butyryl cholinesterase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001540molecular_functionamyloid-beta binding
A0003824molecular_functioncatalytic activity
A0003990molecular_functionacetylcholinesterase activity
A0004104molecular_functioncholinesterase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005641cellular_componentnuclear envelope lumen
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005886cellular_componentplasma membrane
A0006581biological_processacetylcholine catabolic process
A0006805biological_processxenobiotic metabolic process
A0007584biological_processresponse to nutrient
A0007612biological_processlearning
A0008285biological_processnegative regulation of cell population proliferation
A0009410biological_processresponse to xenobiotic stimulus
A0014016biological_processneuroblast differentiation
A0016486biological_processpeptide hormone processing
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0019695biological_processcholine metabolic process
A0019899molecular_functionenzyme binding
A0033265molecular_functioncholine binding
A0042802molecular_functionidentical protein binding
A0043279biological_processresponse to alkaloid
A0050783biological_processcocaine metabolic process
A0050805biological_processnegative regulation of synaptic transmission
A0051384biological_processresponse to glucocorticoid
A0051593biological_processresponse to folic acid
A0052689molecular_functioncarboxylic ester hydrolase activity
A0072562cellular_componentblood microparticle
Functional Information from PROSITE/UniProt
site_idPS00122
Number of Residues16
DetailsCARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGnpksVtLfGeSAG
ChainResidueDetails
APHE185-GLY200

site_idPS00941
Number of Residues11
DetailsCARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWiP
ChainResidueDetails
AGLU90-PRO100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:12869558
ChainResidueDetails
ASER198

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:12869558
ChainResidueDetails
AGLU325
AHIS438

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:4BDS
ChainResidueDetails
ATRP82
AHIS438

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLY116

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22444575
ChainResidueDetails
ASER198

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18203274
ChainResidueDetails
AGLN17
AGLN455

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
ChainResidueDetails
AASN57
AASN341

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
ChainResidueDetails
AASN106

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
ChainResidueDetails
AASN241

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
ChainResidueDetails
AASN256

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3542989
ChainResidueDetails
AGLN481
AGLN486

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:23679855
ChainResidueDetails
AASN485

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qe3
ChainResidueDetails
AGLU325
AHIS438
ASER198

226707

PDB entries from 2024-10-30

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