Structure of PDB 2bis Chain C Binding Site BS02

Receptor Information
>2bis Chain C (length=440) Species: 29292 (Pyrococcus abyssi) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSHMKVLLLGFEFLPVKVGGLAEALTAISEALASLGHEVLVFTPSHGRFQ
GEEIGKIRVFGEEVQVKVSYEERGNLRIYRIGGGLLDSEDVYGPGWDGLI
RKAVTFGRASVLLLNDLLREEPLPDVVHFHDWHTVFAGALIKKYFKIPAV
FTIHRLNKSKLPAFYFHEAGLSELAPYPDIDPEHTGGYIADIVTTVSRGY
LIDEWGFFRNFEGKITYVFNGIDCSFWNESYLTGSRDERKKSLLSKFGMD
EGVTFMFIGRFDRGQKGVDVLLKAIEILSSKKEFQEMRFIIIGKGDPELE
GWARSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALE
AMCLGAIPIASAVGGLRDIITNETGILVKAGDPGELANAILKALELSRSD
LSKFRENCKKRAMSFSWEKSAERYVKAYTGSIDRAFDFIL
Ligand information
Ligand IDUDP
InChIInChI=1S/C9H14N2O12P2/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(22-8)3-21-25(19,20)23-24(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,19,20)(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1
InChIKeyXCCTYIAWTASOJW-XVFCMESISA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)(O)OP(=O)(O)O)O)O
CACTVS 3.370O[CH]1[CH](O)[CH](O[CH]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
CACTVS 3.370O[C@H]1[C@@H](O)[C@@H](O[C@@H]1CO[P](O)(=O)O[P](O)(O)=O)N2C=CC(=O)NC2=O
OpenEye OEToolkits 1.7.0C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)O)O)O
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)C(O)C2O
FormulaC9 H14 N2 O12 P2
NameURIDINE-5'-DIPHOSPHATE
ChEMBLCHEMBL130266
DrugBankDB03435
ZINCZINC000004490939
PDB chain2bis Chain C Residue 603 [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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PDB2bis Crystal Structure of an Archaeal Glycogen Synthase: Insights Into Oligomerisation and Substrate Binding of Eukaryotic Glycogen Synthases.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		F161 H164 E165
Binding residue
(residue number reindexed from 1)		F164 H167 E168
Annotation score2
Enzymatic activity
Enzyme Commision number 2.4.1.21: starch synthase.
Gene Ontology
Molecular Function
GO:0004373 alpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity
GO:0016757 glycosyltransferase activity

View graph for
Molecular Function
External links
PDB RCSB:2bis, PDBe:2bis, PDBj:2bis
PDBsum2bis
PubMed16319074
UniProtQ9V2J8

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