Structure of PDB 2j4h Chain A Binding Site BS02

Receptor Information

>2j4h Chain A (length=174) Species: 562 (Escherichia coli)

MRLCDRDIEAWLDEGRLSINPRPPVERINGATVDVRLGNKFRTFRGHTAA
FIDLSGPKDEVSAALDRVMSDEIVLDEGEAFYLHPGELALAVTLESVTLP
ADLVGWLDGRSSLARLGLMVAVTAHRIDPGWSGCIVLEFYNSGKLPLALR
PGMLIGALSFEPLSGPAVRPYNRR

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: 2j4h Chain A Residue 1177

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2j4h Regulation of Dctp Deaminase from Escherichia Coli by Nonallosteric Dttp Binding to an Inactive Form of the Enzyme
• Resolution: 2.7 Å
• Binding residue (original residue number in PDB): A121 V122 H125
• Binding residue (residue number reindexed from 1): A121 V122 H125
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): S111 R115 A124 R126 E138
• Catalytic site (residue number reindexed from 1): S111 R115 A124 R126 E138
• Enzyme Commision number: 3.5.4.13: dCTP deaminase.

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0008829 dCTP deaminase activity
• GO:0016787 hydrolase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0006226 dUMP biosynthetic process
• GO:0006229 dUTP biosynthetic process
• GO:0006235 dTTP biosynthetic process
• GO:0009117 nucleotide metabolic process
• GO:0009314 response to radiation
• GO:0015949 nucleobase-containing small molecule interconversion
• GO:0070207 protein homotrimerization

Cellular Component

• GO:0005829 cytosol
• GO:0032991 protein-containing complex

External links

• PDB: RCSB:2j4h, PDBe:2j4h, PDBj:2j4h
• PDBsum: 2j4h
• PubMed: 17651436
• UniProt: P28248|DCD_ECOLI dCTP deaminase (Gene Name=dcd)