BioLiP

Structure of PDB 1kdr Chain A

Receptor sequence

>1kdrA (length=221) Species: 562 (Escherichia coli) [Search protein sequence]

AIAPVITIDGPSGAGKGTLCKAMAEALQWHLLDSGAIYRVLALAALHHHV
DVASEDALVPLASHLDVRFVSTNGNLEVILEGEDVSGEIRTQEVANAASQ
VAAFPRVREALLRRQRAFRELPGLIADGRDMGTVVFPDAPVKIFLDASSE
ERAHRRMLQLQEKGFSVNFERLLAEIKERDDRDRNRAVAPLVPAADALVL
DSTTLSIEQVIEKALQYARQK

3D structure

PDB

1kdr Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme.

Chain

Resolution

2.25 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

2.7.4.25: (d)CMP kinase.

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	CAR	A	G37 R41 A104 R110 G130 R131 D185 R188	G35 R39 A102 R108 G128 R129 D183 R186

Gene Ontology

	Molecular Function
GO:0004127	(d)CMP kinase activity
GO:0005524	ATP binding
GO:0016301	kinase activity
GO:0036430	CMP kinase activity
GO:0036431	dCMP kinase activity
GO:0097216	guanosine tetraphosphate binding

	Biological Process
GO:0006139	nucleobase-containing compound metabolic process
GO:0006220	pyrimidine nucleotide metabolic process
GO:0009058	biosynthetic process
GO:0010165	response to X-ray
GO:0015949	nucleobase-containing small molecule interconversion
GO:0016310	phosphorylation
GO:0044281	small molecule metabolic process
GO:0046940	nucleoside monophosphate phosphorylation

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol

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Molecular Function

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Biological Process

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Cellular Component

PDB	RCSB:1kdr, PDBe:1kdr, PDBj:1kdr
PDBsum	1kdr
PubMed	11827479
UniProt	P0A6I0\|KCY_ECOLI Cytidylate kinase (Gene Name=cmk)