Structure of PDB 4jae Chain A

Receptor sequence

>4jaeA (length=426) Species: 83333 (Escherichia coli K-12)

ADTKAKLTLDGDTAVELDVLKGTLGQDVIDIRTLGSKGVFTFDPGFTSTT
SCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQY
DEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLD
VNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNM
MFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFA
CIAAGIASLWGPAHGGANEAALKMLEEIGKKENIPEFVRRAKDKNDSFRL
MGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELENIALNDP
YFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHS
DGMKIARPRQLYTGYEKRDFKSDIKR

3D structure

• PDB: 4jae Enzyme-substrate complexes of allosteric citrate synthase: Evidence for a novel intermediate in substrate binding.
• Chain: A
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D362
• Catalytic site (residue number reindexed from 1): D362
• 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	CMC	A	T106 T108 R109 H110 T111 M112 E158 I159 R163 K167 N189	T106 T108 R109 H110 T111 M112 E158 I159 R163 K167 N189

Gene Ontology

Molecular Function

• GO:0004108 citrate (Si)-synthase activity
• GO:0005515 protein binding
• GO:0016740 transferase activity
• GO:0036440 citrate synthase activity
• GO:0042802 identical protein binding
• GO:0046912 acyltransferase activity, acyl groups converted into alkyl on transfer
• GO:0070404 NADH binding

Biological Process

• GO:0006099 tricarboxylic acid cycle
• GO:0034214 protein hexamerization

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:4jae, PDBe:4jae, PDBj:4jae
• PDBsum: 4jae
• PubMed: 23954305
• UniProt: P0ABH7|CISY_ECOLI Citrate synthase (Gene Name=gltA)