Structure of PDB 4xh5 Chain A

Receptor sequence
>4xh5A (length=391) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence]
FPVVLVINCGSSSIKFSVLDVATCDVLMAGIADGMENAFLSINDKPINLA
HSNYEDALKAIAFELEKRDLTDSVALIGHRIGHGGELFTQSVIITDEIID
NIRRVSPLAPLHNYANLSGIDAARHLFPAVRQVAVFDTSFHQTLAPEAYL
YGLPWEYFSSLGVRRYGFHGTSHRYVSRRAYELLDLDEKDSGLIVAHLGN
GASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMAWIAKETGQTL
SDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERARLAIKTFVHRIAR
HIAGHAASLHRLDGIIFTGGIGENSVLIRQLVIEHLGVLGLTLDVEMNKQ
PNSHGERIISANPSQVICAVIPTNEEKMIALDAIHLGNVKA
3D structure
PDB4xh5 Structures of substrate- and nucleotide-bound propionate kinase from Salmonella typhimurium: substrate specificity and phosphate-transfer mechanism
ChainA
Resolution2.11 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N11 R86 H175 R236 E381
Catalytic site (residue number reindexed from 1) N8 R80 H169 R230 E375
Enzyme Commision number 2.7.2.15: propionate 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 ANP A G205 N206 G207 D278 L279 R280 G326 I327 N330 G199 N200 G201 D272 L273 R274 G320 I321 N324
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008776 acetate kinase activity
GO:0008980 propionate kinase activity
GO:0016301 kinase activity
GO:0016774 phosphotransferase activity, carboxyl group as acceptor
GO:0046872 metal ion binding
Biological Process
GO:0006082 organic acid metabolic process
GO:0006083 acetate metabolic process
GO:0016310 phosphorylation
GO:0070689 L-threonine catabolic process to propionate
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4xh5, PDBe:4xh5, PDBj:4xh5
PDBsum4xh5
PubMed26249345
UniProtO06961|TDCD_SALTY Propionate kinase (Gene Name=tdcD)

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