Structure of PDB 1oh9 Chain A

Receptor sequence

>1oh9A (length=258) Species: 469008 (Escherichia coli BL21(DE3))

MMNPLIIKLGGVLLDSEEALERLFSALVNYRESHQRPLVIVHGGGCVVDE
LMKGLNLPVKKKNGLRVTPADQIDIITGALAGTANKTLLAWAKKHQIAAV
GLFLGDGDSVKVTQLDEELGHVGLAQPGSPKLINSLLENGYLPVVSSIGV
TDEGQLMNVNADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTAAK
AEQLIEQGIITDGMIVKVNAALDAARTLGRPVDIASWRHAEQLPALFNGM
PMGTRILA

3D structure

• PDB: 1oh9 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
• Chain: A
• Resolution: 1.91 Å

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	K8 G10 L186 I209 T211 D212 M214 K217	K8 G10 L186 I209 T211 D212 M214 K217
BS02	NLG	A	G43 G44 R66 L80 N158 N160 A161	G43 G44 R66 L80 N158 N160 A161
BS03	ALF	A	K8 G10 G11	K8 G10 G11

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

External links

• PDB: RCSB:1oh9, PDBe:1oh9, PDBj:1oh9
• PDBsum: 1oh9
• PubMed: 12875848
• UniProt: P0A6C8|ARGB_ECOLI Acetylglutamate kinase (Gene Name=argB)