Structure of PDB 2bty Chain C

Receptor sequence
>2btyC (length=282) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MRIDTVNVLLEALPYIKEFYGKTFVIKFGGSAMKQENAKKAFIQDIILLK
YTGIKPIIVHGGGPAISQMMKDLGIEPVFKNGHRVTDEKTMEIVEMVLVG
KINKEIVMNLNLHGGRAVGICGKDSKLIVAEKETKHGDIGYVGKVKKVNP
EILHALIENDYIPVIAPVGIGEDGHSYNINADTAAAEIAKSLMAEKLILL
TDVDGVLKDGKLISTLTPDEAEELIRDGTVTGGMIPKVECAVSAVRGGVG
AVHIINGGLEHAILLEIFSRKGIGTMIKELEG
3D structure
PDB2bty 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
ChainC
Resolution2.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K27 G30 G63 D182 K237
Catalytic site (residue number reindexed from 1) K27 G30 G63 D182 K237
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 ARG C F19 K196 S214 E266 I267 S269 K271 G274 M276 F19 K196 S214 E266 I267 S269 K271 G274 M276
BS02 NLG C K27 G61 G62 G63 K27 G61 G62 G63
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:2bty, PDBe:2bty, PDBj:2bty
PDBsum2bty
PubMed16376937
UniProtQ9X2A4|ARGB_THEMA Acetylglutamate kinase (Gene Name=argB)

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