Structure of PDB 3bsy Chain B Binding Site BS01

Receptor Information
>3bsy Chain B (length=194) Species: 192222 (Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ARTEKIYIYGASGHGLVCEDVAKNMGYKECIFLDDFKGMKFESTLPKYDF
FIAIGNNEIRKKIYQKISENGFKIVNLIHKSALISPSAIVEENAGILIMP
YVVINAKAKIEKGVILNTSSVIEHECVIGEFSHVSVGAKCAGNVKIGKNC
FLGINSCVLPNLSLADDSILGGGATLVKNQDEKGVFVGVPAKRM
Ligand information
Ligand IDACO
InChIInChI=1S/C23H38N7O17P3S/c1-12(31)51-7-6-25-14(32)4-5-26-21(35)18(34)23(2,3)9-44-50(41,42)47-49(39,40)43-8-13-17(46-48(36,37)38)16(33)22(45-13)30-11-29-15-19(24)27-10-28-20(15)30/h10-11,13,16-18,22,33-34H,4-9H2,1-3H3,(H,25,32)(H,26,35)(H,39,40)(H,41,42)(H2,24,27,28)(H2,36,37,38)/t13-,16-,17-,18+,22-/m1/s1
InChIKeyZSLZBFCDCINBPY-ZSJPKINUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
ACDLabs 10.04O=C(SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O)C
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[CH](O)C(C)(C)CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
FormulaC23 H38 N7 O17 P3 S
NameACETYL COENZYME *A
ChEMBLCHEMBL1230809
DrugBank
ZINCZINC000008551095
PDB chain3bsy Chain B Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3bsy Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		N118 H134 S136 V137 F152 G154 I155 G173 V188 M195
Binding residue
(residue number reindexed from 1)		N117 H133 S135 V136 F151 G153 I154 G172 V187 M194
Annotation score4
Enzymatic activity
Enzyme Commision number 2.3.1.203: UDP-N-acetylbacillosamine N-acetyltransferase.
Gene Ontology
Molecular Function
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006486 protein glycosylation
GO:0018279 protein N-linked glycosylation via asparagine

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3bsy, PDBe:3bsy, PDBj:3bsy
PDBsum3bsy
PubMed18667421
UniProtQ0P9D1|PGLD_CAMJE UDP-N-acetylbacillosamine N-acetyltransferase (Gene Name=pglD)

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