Structure of PDB 2ako Chain D

Receptor sequence
>2akoD (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
ChainD
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 D S162 D163 I164 F167 Y168 N171 P172 T204 G206 I207 K210 S161 D162 I163 F166 Y167 N170 P171 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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