Structure of PDB 2r26 Chain B

Receptor sequence

>2r26B (length=380) Species: 2303 (Thermoplasma acidophilum)

EEISKGLEDVNIKWTRLTTIDGNKGILRYGGYSVEDIIASGAQDEEIQYL
FLYGNLPTEQELRKYKETVQKGYKIPDFVINAIRQLPRESDAVAMQMAAV
AAMAASETKFKWNKDTDRDVAAEMIGRMSAITVNVYRHIMNMPAELPKPS
DSYAESFLNAAFGRKATKEEIDAMNTALILYTDHEVPASTTAGLVAVSTL
SDMYSGITAALAALKGPLHGGAAEAAIAQFDEIKDPAMVEKWFNDNIING
KKRLMGFGHRVYKTYDPRAKIFKGIAEKLSSKKPEVHKVYEIATKLEDFG
IKAFGSKGIYPNTDYFSGIVYMSIGFPLRNNIYTALFALSRVTGWQAHFI
EYVEEQQRLIRPRAVYVGPAERKYVPIAER

3D structure

• PDB: 2r26 The Structure of the Ternary Complex of Carboxymethyl Coenzyme A and Oxalateacetate with Citrate Synthase from the Thermophilic Archaeonthermoplasma Acidophilum
• Chain: B
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S192 H222 H262 R271 D317
• Catalytic site (residue number reindexed from 1): S189 H219 H259 R268 D314
• 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	B	H187 P190 H222 H262 R271 R344	H184 P187 H219 H259 R268 R341
BS02	CMC	B	L221 H222 G223 A225 R256 L257 M258 G259 F260 G261 H262 R263 I312 N315 D317	L218 H219 G220 A222 R253 L254 M255 G256 F257 G258 H259 R260 I309 N312 D314

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

External links

• PDB: RCSB:2r26, PDBe:2r26, PDBj:2r26
• PDBsum: 2r26
• UniProt: P21553|CISY_THEAC Citrate synthase (Gene Name=gltA)