Structure of PDB 1ohb Chain A

Receptor sequence
>1ohbA (length=258) Species: 469008 (Escherichia coli BL21(DE3)) [Search protein sequence]
MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIVHGGGCVVDE
LMKGLNLPVKKKNGLRVTPADQIDIITGALAGTANKTLLAWAKKHQIAAV
GLFLGDGDSVKVTQLDEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGV
TDEGQLMNVNADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAAK
AEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHAEQLPALFNGM
PMGTRILA
3D structure
PDB1ohb The Course of Phosphorus in the Reaction of N-Acetyl-L-Glutamate Kinase, Determined from the Structures of Crystalline Complexes, Including a Complex with an Alf(4)(-) Transition State Mimic
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K8 G11 G45 D162 K217
Catalytic site (residue number reindexed from 1) K8 G11 G45 D162 K217
Enzyme Commision number 2.7.2.8: acetylglutamate 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 A G11 S180 I185 L186 I209 T211 M214 K217 G11 S180 I185 L186 I209 T211 M214 K217
Gene Ontology
Molecular Function
GO:0003991 acetylglutamate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0006526 L-arginine biosynthetic process
GO:0006974 DNA damage response
GO:0016310 phosphorylation
GO:0042450 arginine biosynthetic process via ornithine
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1ohb, PDBe:1ohb, PDBj:1ohb
PDBsum1ohb
PubMed12875848
UniProtP0A6C8|ARGB_ECOLI Acetylglutamate kinase (Gene Name=argB)

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