Structure of PDB 2qx0 Chain B Binding Site BS01

Receptor Information

>2qx0 Chain B (length=159) Species: 632 (Yersinia pestis)

MIRVYIALGSNLAMPLQQVSAAREALAHLPRSRLVACSPLYRTKPLGPQD
QPDFLNAVVALDTSLPPEQLLDHTQAIERNQGRVRKEQRWGPRTLDLDIM
LYGDQVIKTDRLTIPHYGLKAREFMLYPLADIAPDLIFPDGESLSECLKR
VDKNGLVLW

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: 2qx0 Chain B Residue 163

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2qx0 Structure and activity of Yersinia pestis 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase as a novel target for the development of antiplague therapeutics.
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): D96 D98
• Binding residue (residue number reindexed from 1): D96 D98
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): R83 R93 D96 D98
• Catalytic site (residue number reindexed from 1): R83 R93 D96 D98
• Enzyme Commision number: 2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.

Gene Ontology

Molecular Function

• GO:0003848 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009396 folic acid-containing compound biosynthetic process
• GO:0016310 phosphorylation
• GO:0046654 tetrahydrofolate biosynthetic process
• GO:0046656 folic acid biosynthetic process

External links

• PDB: RCSB:2qx0, PDBe:2qx0, PDBj:2qx0
• PDBsum: 2qx0
• PubMed: 18007032
• UniProt: A0A5P8YCA3