Structure of PDB 2ako Chain C

Receptor sequence
>2akoC (length=241) Species: 197 (Campylobacter jejuni) [Search protein sequence]
KRIVVKVGSHVISEENTLSFERLKNLVAFLAKLMEKYEVILVTSAAISAG
HTKLDIDRKNLINKQVLAAIGQPFLISVYNELLAKFNKLGGQILLTGKDF
DSRKATKHAKNAIDMMINLGILPIINENDATAIEEIVFGDNDSLSAYATH
FFDADLLVILSDIDGFYDKNPSEFSDAKRLEKITHIKEEWLHGTGGIVTK
LKAAKFLLEHNKKMFLASGFDLSVAKTFLLEDKQIGGTLFE
3D structure
PDB2ako Crystal structure of Glutamate 5-kinase from Campylobacter jejuni
ChainC
Resolution2.2 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 ADP C H11 S162 D163 I164 F167 Y168 N171 P172 S173 T204 G206 I207 K210 H10 S161 D162 I163 F166 Y167 N170 P171 S172 T194 G196 I197 K200
Gene Ontology
Molecular Function
GO:0004349 glutamate 5-kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
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:2ako, PDBe:2ako, PDBj:2ako
PDBsum2ako
PubMed
UniProtQ9PJ29|PROB_CAMJE Glutamate 5-kinase (Gene Name=proB)

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