Structure of PDB 1a59 Chain A

Receptor sequence
>1a59A (length=377) Species: 56673 (Antarctic bacterium DS2-3R) [Search protein sequence]
EPTIHKGLAGVTADVTAISKVNSDTNSLLYRGYPVQELAAKCSFEQVAYL
LWNSELPNDSELKAFVNFERSHRKLDENVKGAIDLLSTACHPMDVARTAV
SVLGANHARAQDSSPEANLEKAMSLLATFPSVVAYDQRRRRGEELIEPRE
DLDYSANFLWMTFGEEAAPEVVEAFNVSMILYAEHSFNASTFTARVITST
LADLHSAVTGAIGALKGPLHGGANEAVMHTFEEIGIRKDESLDEAATRSK
AWMVDALAQKKKVMGFGHRVYKNGDSRVPTMKSALDAMIKHYDRPEMLGL
YNGLEAAMEEAKQIKPNLDYPAGPTYNLMGFDTEMFTPLFIAARITGWTA
HIMEQVADNALIRPLSEYNGPEQRQVP
3D structure
PDB1a59 Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium.
ChainA
Resolution2.09 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S191 H221 H269 R278 D320
Catalytic site (residue number reindexed from 1) S190 H220 H268 R277 D319
Enzyme Commision number 2.3.3.16: citrate synthase (unknown stereospecificity).
2.3.3.5: 2-methylcitrate 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 COA A L220 A224 K263 V264 M265 G266 F267 G268 H269 R270 I315 N318 L219 A223 K262 V263 M264 G265 F266 G267 H268 R269 I314 N317
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
GO:0050440 2-methylcitrate synthase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006099 tricarboxylic acid cycle
GO:0019679 propionate metabolic process, methylcitrate 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:1a59, PDBe:1a59, PDBj:1a59
PDBsum1a59
PubMed9551556
UniProtO34002|PRPC_ABDS2 2-methylcitrate synthase (Gene Name=gltA)

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