Structure of PDB 2buf Chain D

Receptor sequence
>2bufD (length=294) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
TLSRDDAAQVAKVLSEALPYIRRFVGKTLVIKYGGNAMESEELKAGFARD
VVLMKAVGINPVVVHGGGPQIGDLLKRLSIESHFIDGMRVTDAATMDVVE
MVLGGQVNKDIVNLINRHGGSAIGLTGKDAELIRAKKLTVTRQTKPEIID
IGHVGEVTGVNVGLLNMLVKGDFIPVIAPIGVGSNGESYNINADLVAGKV
AEALKAEKLMLLTNIAGLMDKQGQVLTGLSTEQVNELIADGTIYGGMLPK
IRCALEAVQGGVTSAHIIDGRVPNAVLLEIFTDSGVGTLISNRK
3D structure
PDB2buf 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
ChainD
Resolution2.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K33 G36 G69 D199 K255
Catalytic site (residue number reindexed from 1) K32 G35 G68 D194 K250
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 D T218 N219 I220 M224 T247 Y249 G251 M252 K255 T213 N214 I215 M219 T242 Y244 G246 M247 K250
BS02 NLG D G67 R90 N195 A198 G66 R89 N190 A193
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2buf, PDBe:2buf, PDBj:2buf
PDBsum2buf
PubMed16376937
UniProtQ9HTN2|ARGB_PSEAE Acetylglutamate kinase (Gene Name=argB)

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