Structure of PDB 1mc3 Chain B Binding Site BS01

Receptor Information

>1mc3 Chain B (length=291) Species: 562 (Escherichia coli)

HMKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREI
LIITTPEDKGYFQRLLGDGSEFGIQLEYAEQPSPDGLAQAFIIGETFLNG
EPSCLVLGDNIFFGQGFSPKLRHVAARTEGATVFGYQVMDPERFGVVEFD
DNFRAISLEEKPKQPKSNWAVTGLYFYDSKVVEYAKQVKPSERGELEITS
INQMYLEAGNLTVELLGRGFAWLDTGTHDSLIEASTFVQTVEKRQGFKIA
CLEEIAWRNGWLDDEGVKRAASSLAKTGYGQYLLELLRARP

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 1mc3 Chain B Residue 302

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1mc3 Crystal Structure of Escherichia coli Glucose-1-Phosphate Thymidylyltransferase (RffH) Complexed with dTTP and Mg2+
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): D108 D223
• Binding residue (residue number reindexed from 1): D109 D224
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.7.7.24: glucose-1-phosphate thymidylyltransferase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0008879 glucose-1-phosphate thymidylyltransferase activity
• GO:0016779 nucleotidyltransferase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0000271 polysaccharide biosynthetic process
• GO:0009058 biosynthetic process
• GO:0009243 O antigen biosynthetic process
• GO:0009246 enterobacterial common antigen biosynthetic process
• GO:0045226 extracellular polysaccharide biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1mc3, PDBe:1mc3, PDBj:1mc3
• PDBsum: 1mc3
• PubMed: 12171937
• UniProt: P61887|RMLA2_ECOLI Glucose-1-phosphate thymidylyltransferase 2 (Gene Name=rffH)