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5DYW

Crystal structure of human butyrylcholinesterase in complex with N-((1-benzylpiperidin-3-yl)methyl)-N-(2-methoxyethyl)naphthalene-2-sulfonamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004104molecular_functioncholinesterase activity
B0004104molecular_functioncholinesterase activity
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
AASN17
AASN455
BASN17
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
AASN481
AASN486
BASN481
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

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PDB entries from 2024-10-30

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