Structure of PDB 2buf Chain H

Receptor sequence

>2bufH (length=295) Species: 287 (Pseudomonas aeruginosa)

TLSRDDAAQVAKVLSEALPYIRRFVGKTLVIKYGGNAMESEELKAGFARD
VVLMKAVGINPVVVHGGGPQIGDLLKRLSIESHFIDGMRVTDAATMDVVE
MVLGGQVNKDIVNLINRHGGSAIGLTGKDAELIRAKKLTVTRQTPEMTKP
EIIDIGHVGEVTGVNVGLLNMLVKGDFIPVIAPIGVGSNGESYNINADLV
AGKVAEALKAEKLMLLTNIAGLMDKQGQVLTGLSTEQVNELIADGTIYGG
MLPKIRCALEAVQGGVTSAHIIDGRVPNAVLLEIFTDSGVGTLIS

3D structure

• PDB: 2buf Structural Bases of Feed-Back Control of Arginine Biosynthesis, Revealed by the Structure of Two Hexameric N-Acetylglutamate Kinases, from Thermotoga Maritima and Pseudomonas Aeruginosa
• Chain: H
• Resolution: 2.95 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K33 G36 G69 D199 K255
• Catalytic site (residue number reindexed from 1): K32 G35 G68 D198 K254
• 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	H	I220 G222 L223 M224 T247 Y249 G251 M252 K255	I219 G221 L222 M223 T246 Y248 G250 M251 K254
BS02	NLG	H	G67 G69 R90 N195 N197 A198	G66 G68 R89 N194 N196 A197

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:0016310 phosphorylation
• GO:0042450 arginine biosynthetic process via ornithine

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2buf, PDBe:2buf, PDBj:2buf
• PDBsum: 2buf
• PubMed: 16376937
• UniProt: Q9HTN2|ARGB_PSEAE Acetylglutamate kinase (Gene Name=argB)