Structure of PDB 2r26 Chain D

Receptor sequence
>2r26D (length=379) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
EISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASGAQDEEIQYLF
LYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESDAVAMQMAAVA
AMAASETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPSD
SYAESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTLS
DMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWFNDNIINGK
KRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVHKVYEIATKLEDFGI
KAFGSKGIYPNTDYFSGIVYMSIGFPLRNNIYTALFALSRVTGWQAHFIE
YVEEQQRLIRPRAVYVGPAERKYVPIAER
3D structure
PDB2r26 The Structure of the Ternary Complex of Carboxymethyl Coenzyme A and Oxalateacetate with Citrate Synthase from the Thermophilic Archaeonthermoplasma Acidophilum
ChainD
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) 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 OAA D H187 P190 H222 H262 R271 F340 R344 H183 P186 H218 H258 R267 F336 R340
BS02 CMC D L221 H222 A225 R256 L257 M258 G259 F260 G261 H262 R263 K310 I312 N315 D317 L217 H218 A221 R252 L253 M254 G255 F256 G257 H258 R259 K306 I308 N311 D313
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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