Structure of PDB 2j4q Chain A

Receptor sequence
>2j4qA (length=174) Species: 562 (Escherichia coli) [Search protein sequence]
MRLCDRDIEAWLDEGRLSINPRPPVERINGATVDVRLGNKFRTFRGHTAA
FIDLSGPKDEVSAALDRVMSDEIVLDEGEAFYLHPGELALAVTLESVTLP
ADLVGWLDGRSSLARLGLMVHVTAHRIDPGWSGCIVLAFYNSGKLPLALR
PGMLIGALSFEPLSGPAVRPYNRR
3D structure
PDB2j4q Regulation of Dctp Deaminase from Escherichia Coli by Nonallosteric Dttp Binding to an Inactive Form of the Enzyme
ChainA
Resolution2.6 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 TYD A H121 A124 R126 D128 I135 V136 Y171 H121 A124 R126 D128 I135 V136 Y171
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2j4q, PDBe:2j4q, PDBj:2j4q
PDBsum2j4q
PubMed17651436
UniProtP28248|DCD_ECOLI dCTP deaminase (Gene Name=dcd)

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