Structure of PDB 1e19 Chain B

Receptor sequence
>1e19B (length=313) Species: 2261 (Pyrococcus furiosus) [Search protein sequence]
GKRVVIALGGNALQQRGQKGSYEEMMDNVRKTARQIAEIIARGYEVVITH
GNGPQVGSLLLHMDAGQATYGIPAQPMDVAGAMSQGWIGYMIQQALKNEL
RKRGMEKKVVTIITQTIVDKNDPAFQNPTKPVGPFYDEETAKRLAREKGW
IVKEDSGRGWRRVVPSPDPKGHVEAETIKKLVERGVIVIASGGGGVPVIL
EDGEIKGVEAVIDKDLAGEKLAEEVNADIFMILTDVNGAALYYGTEKEQW
LREVKVEELRKYYEEGHFKAGSMGPKVLAAIRFIEWGGERAIIAHLEKAV
EALEGKTGTQVLP
3D structure
PDB1e19 The 1.5-A Resolution Crystal Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase from the Hyperthermophilic Archaeon Pyrococcus Furiosus, Bound to Adp, Confirms that This Thermoestable Enzyme is a Carbamate Kinase, and Provides Insights Into Substrate Binding and Stability in Carbamate Kinases
ChainB
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G11 N12 K131 K215 K277
Catalytic site (residue number reindexed from 1) G10 N11 K130 K214 K276
Enzyme Commision number 2.7.2.2: carbamate 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 B G11 T235 D236 V237 A241 Y244 H268 K270 S273 M274 K277 G10 T234 D235 V236 A240 Y243 H267 K269 S272 M273 K276
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008804 carbamate kinase activity
GO:0016301 kinase activity
Biological Process
GO:0006525 arginine metabolic process
GO:0016310 phosphorylation
GO:0019546 arginine deiminase pathway
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:1e19, PDBe:1e19, PDBj:1e19
PDBsum1e19
PubMed10860751
UniProtP95474|CPKA_PYRFU Carbamate kinase (Gene Name=cpkA)

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