Structure of PDB 1aj8 Chain B

Receptor sequence
>1aj8B (length=370) Species: 2261 (Pyrococcus furiosus) [Search protein sequence]
LAKGLEDVYIDQTNICYIDGKEGKLYYRGYSVEELAELSTFEEVVYLLWW
GKLPSLSELENFKKELAKSRGLPKEVIEIMEALPKNTHPMGALRTIISYL
GNIDDSGDIPVTPEEVYRIGISVTAKIPTIVANWYRIKNGLEYVPPKEKL
SHAANFLYMLHGEEPPKEWEKAMDVALILYAEHEINASTLAVMTVGSTLS
DYYSAILAGIGALKGPIHGGAVEEAIKQFMEIGSPEKVEEWFFKALQQKR
KIMGAGHRVYKTYDPRARIFKKYASKLGDKKLFEIAERLERLVEEYLSKK
GISINVDYWSGLVFYGMKIPIELYTTIFAMGRIAGWTAHLAEYVSHNRII
RPRLQYVGEIGKKYLPIELR
3D structure
PDB1aj8 The crystal structure of citrate synthase from the hyperthermophilic archaeon pyrococcus furiosus at 1.9 A resolution,.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S193 H223 H262 R271 D312
Catalytic site (residue number reindexed from 1) S188 H218 H257 R266 D307
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 COA B I222 A226 K256 I257 M258 G259 A260 G261 R263 K305 I307 N310 I217 A221 K251 I252 M253 G254 A255 G256 R258 K300 I302 N305
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1aj8, PDBe:1aj8, PDBj:1aj8
PDBsum1aj8
PubMed9254593
UniProtQ53554|CISY_PYRFU Citrate synthase (Gene Name=gltA)

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