Structure of PDB 1xs6 Chain D

Receptor sequence
>1xs6D (length=193) Species: 562 (Escherichia coli) [Search protein sequence]
MRLCDRDIEAWLDEGRLSINPRPPVERINGATVDVRLGNKFRTFRGHTAA
FIDLSGPKDEVSAALDRVMSDEIVLDEGEAFYLHPGELALAVTLESVTLP
ADLVGWLDGRSSLARLGLMVHVTAHRIDPGWSGCIVLAFYNSGKLPLALR
PGMLIGALSFEPLSGPAVRPYNRREDAKYRNQQGAVASRIDKD
3D structure
PDB1xs6 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
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 D A124 R126 D128 W131 I135 V136 Y171 R174 A177 K178 A124 R126 D128 W131 I135 V136 Y171 R174 A177 K178
BS02 DUT D 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

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Cellular Component
External links
PDB RCSB:1xs6, PDBe:1xs6, PDBj:1xs6
PDBsum1xs6
PubMed15539408
UniProtP28248|DCD_ECOLI dCTP deaminase (Gene Name=dcd)

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