Structure of PDB 2j5t Chain C

Receptor sequence
>2j5tC (length=356) Species: 562 (Escherichia coli) [Search protein sequence]
DSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGA
IAAGREHLGYPELPATIASKQLLAAVGQSRLIQLWEQLFSIYGIHVGQML
LTRADMEDRERFLNARDTLRALLDNNVVPVINENDAVATAEIKVGDNDNL
SALAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIA
GGMSTKLQAADVACRAGIDTIIAAGSKPGVIGDVMEGISVGTLFHAQATP
LENRKRWIFGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGE
VIRICNLEGRDIAHGVSRYNSDALRRIAGHHSQEIDAILGYEYGPVAVHR
DDMITR
3D structure
PDB2j5t A Novel Two-Domain Architecture within the Amino Acid Kinase Enzyme Family Revealed by the Crystal Structure of Escherichia Coli Glutamate 5-Kinase.
ChainC
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.2.11: glutamate 5-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 GLU C S50 G51 A52 D137 D148 N149 S48 G49 A50 D135 D146 N147
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003723 RNA binding
GO:0004349 glutamate 5-kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:1901973 proline binding
Biological Process
GO:0006561 proline biosynthetic process
GO:0008652 amino acid biosynthetic process
GO:0016310 phosphorylation
GO:0055129 L-proline biosynthetic process
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:2j5t, PDBe:2j5t, PDBj:2j5t
PDBsum2j5t
PubMed17321544
UniProtP0A7B5|PROB_ECOLI Glutamate 5-kinase (Gene Name=proB)

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