Structure of PDB 2c6x Chain B

Receptor sequence
>2c6xB (length=363) Species: 1423 (Bacillus subtilis) [Search protein sequence]
VHYGLKGITCVETSISHIDGEKGRLIYRGHHAKDIALNHSFEEAAYLILF
GKLPSTEELQVFKDKLAAERNLPEHIERLIQSLPNNMDDMSVLRTVVSAL
GENTYTFHPKTEEAIRLIAITPSIIAYRKRWTRGEQAIAPSSQYGHVENY
YYMLTGEQPSEAKKKALETYMILATEHGMNASTFSARVTLSTESDLVSAV
TAALGTMKGPLHGGAPSAVTKMLEDIGEKEHAEAYLKEKLEKGERLMGFG
HRVYKTKDPRAEALRQKAEEVAGNDRDLDLALHVEAEAIRLLEIYKPGRK
LYTNVEFYAAAVMRAIDFDDELFTPTFSASRMVGWCAHVLEQAENNMIFR
PSAQYTGAIPEEV
3D structure
PDB2c6x Domain Closure in Citrate Synthases Adapted to the Range of Biological Temperatures
ChainB
Resolution3.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S183 H213 H252 R261 E307
Catalytic site (residue number reindexed from 1) S182 H212 H251 R260 E306
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 COZ B R246 L247 M248 F250 G251 K297 R300 L302 E307 R245 L246 M247 F249 G250 K296 R299 L301 E306
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2c6x, PDBe:2c6x, PDBj:2c6x
PDBsum2c6x
PubMed
UniProtP39119|CISY_BACSU Citrate synthase 1 (Gene Name=citA)

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