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3O9M

Co-crystallization studies of full length recombinant BChE with cocaine offers insights into cocaine detoxification

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
A0016787molecular_functionhydrolase activity
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
B0001540molecular_functionamyloid-beta binding
B0003824molecular_functioncatalytic activity
B0003990molecular_functionacetylcholinesterase activity
B0004104molecular_functioncholinesterase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005641cellular_componentnuclear envelope lumen
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005886cellular_componentplasma membrane
B0006581biological_processacetylcholine catabolic process
B0006805biological_processxenobiotic metabolic process
B0007584biological_processresponse to nutrient
B0007612biological_processlearning
B0008285biological_processnegative regulation of cell population proliferation
B0009410biological_processresponse to xenobiotic stimulus
B0014016biological_processneuroblast differentiation
B0016486biological_processpeptide hormone processing
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0019695biological_processcholine metabolic process
B0019899molecular_functionenzyme binding
B0033265molecular_functioncholine binding
B0042802molecular_functionidentical protein binding
B0043279biological_processresponse to alkaloid
B0050783biological_processcocaine metabolic process
B0050805biological_processnegative regulation of synaptic transmission
B0051384biological_processresponse to glucocorticoid
B0051593biological_processresponse to folic acid
B0052689molecular_functioncarboxylic ester hydrolase activity
B0072562cellular_componentblood microparticle
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BEZ A 999
ChainResidue
AGLY116
AGLY117
ASER198
ALEU286
AHIS438

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BEZ B 999
ChainResidue
BGLY116
BGLY117
BSER198
BHIS438

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 Residues2
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4BDS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22444575","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15667209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17355286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17768338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18975951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15667209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17355286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17768338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18975951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15667209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17355286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"18203274","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18975951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3542989","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12869558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15667209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17355286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17768338","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18975951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19368529","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23679855","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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