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2WIL

AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN ANALOGUE TA5

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
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
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 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
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039, ECO:0000269|PubMed:12869558
ChainResidueDetails
ASER198
BSER198

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:12869558
ChainResidueDetails
AGLU325
AHIS438
BGLU325
BHIS438

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:4BDS
ChainResidueDetails
ATRP82
AHIS438
BTRP82
BHIS438

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLY116
BGLY116

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22444575
ChainResidueDetails
ASER198
BSER198

site_idSWS_FT_FI6
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:18203274
ChainResidueDetails
AGLN17
AASN455
BGLN17
BASN455

site_idSWS_FT_FI7
Number of Residues4
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
BASN57
BASN341

site_idSWS_FT_FI8
Number of Residues2
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
BASN106

site_idSWS_FT_FI9
Number of Residues2
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
BASN241

site_idSWS_FT_FI10
Number of Residues2
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
BASN256

site_idSWS_FT_FI11
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3542989
ChainResidueDetails
AGLN481
AASN486
BGLN481
BASN486

site_idSWS_FT_FI12
Number of Residues2
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
BASN485

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

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qe3
ChainResidueDetails
BGLU325
BHIS438
BSER198

226707

PDB entries from 2024-10-30

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