Structure of PDB 2feo Chain A

Receptor sequence
>2feoA (length=221) Species: 562 (Escherichia coli) [Search protein sequence]
AIAPVITIDGPSGAGKGTLCKAMAEALQWHLLDSGAIYRVLALAALHHHV
DVASEDALVPLASHLDVRFVSTNGNLEVILEGEDVSGEIRTQEVANAASQ
VAAFPRVREALLRRQRAFRELPGLIADGRDMGTVVFPDAPVKIFLDASSE
ERAHRRMLQLQEKGFSVNFERLLAEIKERDDRDRNMAVAPLVPAADALVL
DSTTLSIEQVIEKALQYARQK
3D structure
PDB2feo Structural and functional consequences of single amino acid substitutions in the pyrimidine base binding pocket of Escherichia coli CMP kinase.
ChainA
Resolution2.8 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 DC A G37 R41 A100 S101 G130 R131 G35 R39 A98 S99 G128 R129
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
External links
PDB RCSB:2feo, PDBe:2feo, PDBj:2feo
PDBsum2feo
PubMed17542990
UniProtP0A6I0|KCY_ECOLI Cytidylate kinase (Gene Name=cmk)

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