Structure of PDB 2bmu Chain A Binding Site BS03

Receptor Information

>2bmu Chain A (length=225) Species: 2261 (Pyrococcus furiosus)

MRIVFDIGGSVLVPENPDIDFIKEIAYQLTKVSEDHEVAVVVGGGKLARK
YIEVAEKFNSSETFKDFIGIQITRANAMLLIAALREKAYPVVVEDFWEAW
KAVQLKKIPVMGGTHPGHTTDAVAALLAEFLKADLLVVITNVDGVYTADP
KKDPTAKKIKKMKPEELLEIVGKGIEKAGSSSVIDPLAAKIIARSGIKTI
VIGKEDAKDLFRVIKGDHNGTTIEP

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: 2bmu Chain A Residue 1228

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2bmu The Crystal Structure of Pyrococcus Furiosus Ump Kinase Provides Insight Into Catalysis and Regulation in Microbial Pyrimidine Nucleotide Biosynthesis.
• Resolution: 2.55 Å
• Binding residue (original residue number in PDB): D6 T120
• Binding residue (residue number reindexed from 1): D6 T120
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.7.4.22: UMP kinase.

Gene Ontology

Molecular Function

• GO:0005524 ATP binding
• GO:0009041 UMP/dUMP kinase activity
• GO:0016301 kinase activity
• GO:0033862 UMP kinase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006221 pyrimidine nucleotide biosynthetic process
• GO:0006225 UDP biosynthetic process
• GO:0016310 phosphorylation
• GO:0044210 'de novo' CTP biosynthetic process
• GO:0046940 nucleoside monophosphate phosphorylation

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2bmu, PDBe:2bmu, PDBj:2bmu
• PDBsum: 2bmu
• PubMed: 16095620
• UniProt: Q8U122|PYRH_PYRFU Uridylate kinase (Gene Name=pyrH)