Structure of PDB 1xs6 Chain A

Receptor sequence

>1xs6A (length=193) Species: 562 (Escherichia coli)

MRLCDRDIEAWLDEGRLSINPRPPVERINGATVDVRLGNKFRTFRGHTAA
FIDLSGPKDEVSAALDRVMSDEIVLDEGEAFYLHPGELALAVTLESVTLP
ADLVGWLDGRSSLARLGLMVHVTAHRIDPGWSGCIVLAFYNSGKLPLALR
PGMLIGALSFEPLSGPAVRPYNRREDAKYRNQQGAVASRIDKD

3D structure

• PDB: 1xs6 Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S111 R115 A124 R126 A138
• Catalytic site (residue number reindexed from 1): S111 R115 A124 R126 A138
• Enzyme Commision number: 3.5.4.13: dCTP deaminase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	DUT	A	A124 R126 D128 W131 I135 V136 Y171 A177 K178	A124 R126 D128 W131 I135 V136 Y171 A177 K178
BS02	DUT	A	R110 S111 S112	R110 S111 S112

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:1xs6, PDBe:1xs6, PDBj:1xs6
• PDBsum: 1xs6
• PubMed: 15539408
• UniProt: P28248|DCD_ECOLI dCTP deaminase (Gene Name=dcd)