Structure of PDB 2r26 Chain A

Receptor sequence
>2r26A (length=381) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
TEEISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASGAQDEEIQY
LFLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESDAVAMQMAA
VAAMAASETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKP
SDSYAESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVST
LSDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWFNDNIIN
GKKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVHKVYEIATKLEDF
GIKAFGSKGIYPNTDYFSGIVYMSIGFPLRNNIYTALFALSRVTGWQAHF
IEYVEEQQRLIRPRAVYVGPAERKYVPIAER
3D structure
PDB2r26 The Structure of the Ternary Complex of Carboxymethyl Coenzyme A and Oxalateacetate with Citrate Synthase from the Thermophilic Archaeonthermoplasma Acidophilum
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S192 H222 H262 R271 D317
Catalytic site (residue number reindexed from 1) S190 H220 H260 R269 D315
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 OAA A H187 P190 H222 H262 R271 R344 H185 P188 H220 H260 R269 R342
BS02 CMC A L221 H222 G223 A225 R256 L257 G259 F260 G261 H262 R263 N315 D317 L219 H220 G221 A223 R254 L255 G257 F258 G259 H260 R261 N313 D315
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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Cellular Component
External links
PDB RCSB:2r26, PDBe:2r26, PDBj:2r26
PDBsum2r26
PubMed
UniProtP21553|CISY_THEAC Citrate synthase (Gene Name=gltA)

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