Structure of PDB 1al6 Chain A

Receptor sequence
>1al6A (length=435) Species: 9031 (Gallus gallus) [Search protein sequence]
STNLKDVLASLIPKEQARIKTFRQQHGNTAVGQITVDMSYGGMRGMKGLI
YETSVLDPDEGIRFRGFSIPECQKLLPKAGGGEEPLPEGLFWLLVTGQIP
TPEQVSWVSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSES
NFARAYAEGINRTKYWEFVYEDAMDLIAKLPCVAAKIYRNLYRAGSSIGA
IDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVG
SALSDPYLSFAAAMNGLAGPLHGLANQEVLLWLSQLQKDLGADASDEKLR
DYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPSDPMFKLVAQ
LYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRA
LGVLAQLIWSRALGFPLERPKSMSTAGLEKLSAGG
3D structure
PDB1al6 Crystallographic Refinement and Atomic Models of Two Different Forms of Citrate Synthase at 2.7 And 1.7 A Resolution
ChainA
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) S244 H274 H320 R329 D375
Catalytic site (residue number reindexed from 1) S242 H272 H318 R327 D373
Enzyme Commision number 2.3.3.1: citrate (Si)-synthase.
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 H238 N242 H274 H320 R329 R401 H236 N240 H272 H318 R327 R399
BS02 HAX A R46 L273 H274 G275 A277 V314 V315 G317 Y318 G319 H320 A321 K366 A367 K368 N373 D375 F397 R44 L271 H272 G273 A275 V312 V313 G315 Y316 G317 H318 A319 K364 A365 K366 N371 D373 F395
Gene Ontology
Molecular Function
GO:0004108 citrate (Si)-synthase activity
GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0006101 citrate metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1al6, PDBe:1al6, PDBj:1al6
PDBsum1al6
PubMed
UniProtP23007|CISY_CHICK Citrate synthase, mitochondrial (Gene Name=CS)

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