Structure of PDB 2h12 Chain E

Receptor sequence
>2h12E (length=426) Species: 435 (Acetobacter aceti) [Search protein sequence]
STATISVDGKSAEMPVLSGTLGPDVIDIRKLPAQLGVFTFDPGYGETAAC
NSKITFIDGDKGVLLHRGYPIAQLAENASYEEVIYLLLNGELPNKAQYDT
FTNTLTNHTLLHEQIRNFFNGFRRDAHPMAILCGTVGALSAFYPDANDIA
IPANRDLAAMRLIAKIPTIAAWAYKYTQGEAFIYPRNDLNYAENFLSMMF
ARMSEPYKVNPVLARAMNRILILHADHEQNASTSTVRLAGSTGANPFACI
AAGIAALWGPAHGGANEAVLKMLARIGKKENIPAFIAQVKDKNSGVKLMG
FGHRVYKNFDPRAKIMQQTCHEVLTELGIKDDPLLDLAVELEKIALSDDY
FVQRKLYPNVDFYSGIILKAMGIPTSMFTVLFAVARTTGWVSQWKEMIEE
PGQRISRPRQLYIGAPQRDYVPLAKR
3D structure
PDB2h12 Structure of a NADH-insensitive hexameric citrate synthase that resists acid inactivation.
ChainE
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S242 H272 H313 R322 D371
Catalytic site (residue number reindexed from 1) S232 H262 H303 R312 D361
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 E H237 N240 H272 H313 R322 R396 H227 N230 H262 H303 R312 R386 MOAD: Kd=21.1uM
BS02 CMX E A271 H272 A275 L308 G310 F311 G312 H313 R314 Y360 R364 L366 N369 D371 A261 H262 A265 L298 G300 F301 G302 H303 R304 Y350 R354 L356 N359 D361
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:0006099 tricarboxylic acid cycle
Cellular Component
GO:0005737 cytoplasm

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Biological Process
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Cellular Component
External links
PDB RCSB:2h12, PDBe:2h12, PDBj:2h12
PDBsum2h12
PubMed17087502
UniProtP20901|CISY_ACEAC Citrate synthase (Gene Name=aarA)

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