Structure of PDB 1ex2 Chain A Binding Site BS03

Receptor Information

>1ex2 Chain A (length=185) Species: 1423 (Bacillus subtilis)

MTKPLILASQSPRRKELLDLLQLPYSIIVSEVEEKLNRNFSPEENVQWLA
KQKAKAVADLHPHAIVIGADTMVCLDGECLGKPQDQEEAASMLRRLSGRS
HSVITAVSIQAENHSETFYDKTEVAFWSLSEEEIWTYIETKEPMDKAGAY
GIQGRGALFVKKIDGDYYSVMGLPISKTMRALRHF

Ligand information

• Ligand ID: PO4
• InChI: InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
• InChIKey: NBIIXXVUZAFLBC-UHFFFAOYSA-K
• SMILES:
  CACTVS 3.341: [O-][P]([O-])([O-])=O
  ACDLabs 10.04: [O-]P([O-])([O-])=O
  OpenEye OEToolkits 1.5.0: [O-]P(=O)([O-])[O-]
• Formula: O4 P
• Name: PHOSPHATE ION
• DrugBank: DB14523
• PDB chain: 1ex2 Chain A Residue 203

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1ex2 Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP.
• Resolution: 1.85 Å
• Binding residue (original residue number in PDB): K51 K55
• Binding residue (residue number reindexed from 1): K51 K55
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.6.1.9: nucleotide diphosphatase.

Gene Ontology

Molecular Function

• GO:0016462 pyrophosphatase activity
• GO:0016787 hydrolase activity
• GO:0036218 dTTP diphosphatase activity
• GO:0036221 UTP diphosphatase activity
• GO:0047429 nucleoside triphosphate diphosphatase activity

Biological Process

• GO:0009117 nucleotide metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1ex2, PDBe:1ex2, PDBj:1ex2
• PDBsum: 1ex2
• PubMed: 10841541
• UniProt: Q02169|NTPPA_BACSU dTTP/UTP pyrophosphatase (Gene Name=maf)