Structure of PDB 3c4q Chain B Binding Site BS02

Receptor Information
>3c4q Chain B (length=393) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRVAMISMHTSPLQQPGTGDSGGMNVYILSTATELAKQGIEVDIYTRATR
PSQGEIVRVAENLRVINIAAGPYEGLSKEELPTQLAAFTGGMLSFTRREK
VTYDLIHSHYWLSGQVGWLLRDLWRIPLIHTAHTLAAVSDTPESEARRIC
EQQLVDNADVLAVNTQEEMQDLMHHYDADPDRISVVSPGADVELYSPGND
RATERSRRELGIPLHTKVVAFVGRLQPFKGPQVLIKAVAALFDRDPDRNL
RVIICGGPYRHMAEELGVEKRIRFLDPRPPSELVAVYRAADIVAVPSFNE
SFGLVAMEAQASGTPVIAARVGGLPIAVAEGETGLLVDGHSPHAWADALA
TLLDDDETRIRMGEDAVEHARTFSWAATAAQLSSLYNDAIANE
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 chain3c4q Chain B Residue 600 [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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PDB3c4q Structural and Enzymatic Analysis of MshA from Corynebacterium glutamicum: SUBSTRATE-ASSISTED CATALYSIS
Resolution2.8 Å
Binding residue
(original residue number in PDB)		Q15 P16 G23 V229 R231 K236 P293 R294 L299 L320 V321 E324
Binding residue
(residue number reindexed from 1)		Q15 P16 G23 V222 R224 K229 P277 R278 L283 L304 V305 E308
Annotation score3
Enzymatic activity
Enzyme Commision number 2.4.1.250: D-inositol-3-phosphate glycosyltransferase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008375 acetylglucosaminyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0016758 hexosyltransferase activity
GO:0046872 metal ion binding
GO:0102710 D-inositol-3-phosphate glycosyltransferase activity
Biological Process
GO:0010125 mycothiol biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3c4q, PDBe:3c4q, PDBj:3c4q
PDBsum3c4q
PubMed18390549
UniProtQ8NTA6|MSHA_CORGL D-inositol 3-phosphate glycosyltransferase (Gene Name=mshA)

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