Structure of PDB 2buf Chain I

Receptor sequence
>2bufI (length=288) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
TLSRDDAAQVAKVLSEALPYIRRFVGKTLVIKYGGNAMESEELKAGFARD
VVLMKAVGINPVVVHGGGPQIGDLLKRLSIESHFIDGMRVTDAATMDVVE
MVLGGQVNKDIVNLINRHGGSAIGLTGKDAELIRAKKLTVTREIIDIGHV
GEVTGVNVGLLNMLVKGDFIPVIAPIGVGSNGESYNINADLVAGKVAEAL
KAEKLMLLTNIAGLMDKQGQVLTGLSTEQVNELIADGTIYGGMLPKIRCA
LEAVQGGVTSAHIIDGRVPNAVLLEIFTDSGVGTLISN
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
ChainI
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 D190 K246
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 I N37 T218 L223 M224 Y249 G251 M252 K255 N36 T209 L214 M215 Y240 G242 M243 K246
BS02 NLG I I72 R90 N195 I196 N197 A198 I71 R89 N186 I187 N188 A189
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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