Structure of PDB 2r9e Chain C

Receptor sequence
>2r9eC (length=379) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
EISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASGAQDEEIQYLF
LYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESDAVAMQMAAVA
AMAASETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSD
SYAESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLS
DMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWFNDNIINGK
KRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVHKVYEIATKLEDFGI
KAFGSKGIYPNTDYFSGIVYMSIGFPLRNNIYTALFALSRVTGWQAHFIE
YVEEQQRLIRPRAVYVGPAERKYVPIAER
3D structure
PDB2r9e Snapshots of Intermediates in the Condensation Reaction Catalyzed by Citrate Synthase
ChainC
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S192 H222 H262 R271 D317
Catalytic site (residue number reindexed from 1) S188 H218 H258 R267 D313
Enzyme Commision number 2.3.3.16: citrate synthase (unknown stereospecificity).
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 SDX C H187 P190 L221 H222 A225 R256 L257 M258 G259 F260 G261 H262 R263 R271 I312 N315 D317 F340 R344 H183 P186 L217 H218 A221 R252 L253 M254 G255 F256 G257 H258 R259 R267 I308 N311 D313 F336 R340
BS02 SDX C R361 R364 R357 R360
Gene Ontology
Molecular Function
GO:0004108 citrate (Si)-synthase activity
GO:0016740 transferase activity
GO:0036440 citrate synthase activity
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006099 tricarboxylic acid cycle
Cellular Component
GO:0005737 cytoplasm
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:2r9e, PDBe:2r9e, PDBj:2r9e
PDBsum2r9e
PubMed
UniProtP21553|CISY_THEAC Citrate synthase (Gene Name=gltA)

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