Structure of PDB 4b0h Chain A Binding Site BS02

Receptor Information

>4b0h Chain A (length=130) Species: 1423 (Bacillus subtilis)

TMQIKIKYLDETQTRISKIEQGDWIDLRAAEDVTIKKDEFKLVPLGVAME
LPEGYEAHVVPRSSTYKNFGVIQTNSMGVIDESYKGDNDFWFFPAYALRD
TEIKKGDRICQFRIMKKMPAVELVEVEHLG

Ligand information

• Ligand ID: POP
• InChI: InChI=1S/H4O7P2/c1-8(2,3)7-9(4,5)6/h(H2,1,2,3)(H2,4,5,6)/p-2
• InChIKey: XPPKVPWEQAFLFU-UHFFFAOYSA-L
• SMILES:
  OpenEye OEToolkits 1.5.0: O[P@@](=O)([O-])O[P@@](=O)(O)[O-]
  CACTVS 3.341: O[P]([O-])(=O)O[P](O)([O-])=O
  ACDLabs 10.04: [O-]P(=O)(O)OP([O-])(=O)O
  OpenEye OEToolkits 1.5.0: OP(=O)([O-])OP(=O)(O)[O-]
• Formula: H2 O7 P2
• Name: PYROPHOSPHATE 2-
• PDB chain: 4b0h Chain B Residue 1146

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4b0h Tying Down the Arm in Bacillus Dutpase: Structure and Mechanism
• Resolution: 1.18 Å
• Binding residue (original residue number in PDB): R63 S64 S65
• Binding residue (residue number reindexed from 1): R62 S63 S64
• Annotation score: 5

Enzymatic activity

• Enzyme Commision number: 3.6.1.23: dUTP diphosphatase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004170 dUTP diphosphatase activity
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006226 dUMP biosynthetic process
• GO:0009117 nucleotide metabolic process
• GO:0046081 dUTP catabolic process

External links

• PDB: RCSB:4b0h, PDBe:4b0h, PDBj:4b0h
• PDBsum: 4b0h
• PubMed: 23897460
• UniProt: O31801|YNCF_BACSU Deoxyuridine 5'-triphosphate nucleotidohydrolase YncF (Gene Name=yncF)