Structure of PDB 1owb Chain A

Receptor sequence

>1owbA (length=426) Species: 562 (Escherichia coli)

ADTKAKLTLNGDTAVELDVLKGTLGQDVIDIRTLGSKGVFTFDPGFTSTA
SCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQY
DEFKTTVTLHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLD
VNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNM
MFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFA
CIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFFRRAKDKNDSFRL
MGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELENIALNDP
YFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHS
DGMKIARPRQLYTGYEKRDFKSDIKR

3D structure

• PDB: 1owb Probing the roles of key residues in the unique regulatory NADH binding site of type II citrate synthase of Escherichia coli.
• Chain: A
• Resolution: 2.2 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	NAD	A	T108 L109 H110 T111 M112 H114 Y145 I159 F162 R163 K167 N189	T108 L109 H110 T111 M112 H114 Y145 I159 F162 R163 K167 N189	MOAD: Kd=1.16uM

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:1owb, PDBe:1owb, PDBj:1owb
• PDBsum: 1owb
• PubMed: 12824188
• UniProt: P0ABH7|CISY_ECOLI Citrate synthase (Gene Name=gltA)