Structure of PDB 3pkp Chain J Binding Site BS02

Receptor Information

>3pkp Chain J (length=289) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium)

KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRD
ILIISTPQDTPRFQQLLGDGSQWGLNLQYKVSPSPDGLAQAFIIGEEFIG
HDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEF
DQKGTAVSLEEKPLQPKSNYAVTGLYFYDNSVVEMAKNLKPSARGELEIT
DINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKV
SCPEEIAFRKNFINAQQVIELAGPLSKNDYGKYLLKMVK

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: 3pkp Chain J Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3pkp Expanding the Nucleotide and Sugar 1-Phosphate Promiscuity of Nucleotidyltransferase RmlA via Directed Evolution.
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): D111 D226
• Binding residue (residue number reindexed from 1): D110 D225
• 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:0046872 metal ion binding

Biological Process

• GO:0009058 biosynthetic process
• GO:0009103 lipopolysaccharide biosynthetic process
• GO:0009243 O antigen biosynthetic process
• GO:0019305 dTDP-rhamnose biosynthetic process
• GO:0045226 extracellular polysaccharide biosynthetic process

External links

• PDB: RCSB:3pkp, PDBe:3pkp, PDBj:3pkp
• PDBsum: 3pkp
• PubMed: 21317292
• UniProt: P26393|RMLA_SALTY Glucose-1-phosphate thymidylyltransferase (Gene Name=rmlA)