Structure of PDB 1nxg Chain A

Receptor sequence
>1nxgA (length=426) Species: 562 (Escherichia coli) [Search protein sequence]
ADTKAKLTLNGDTAVELDVLKGTLGQDVIDIRTLGSKGVFTFDPGFTSTA
SCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQY
DEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLD
VNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNM
MFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFA
CIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFFRRAKDKNDSFRL
MGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELENIALNDP
YFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIAAMARTVGWIAHWSEMHS
DGMKIARPRQLYTGYEKRDFKSDIKR
3D structure
PDB1nxg Insights into the evolution of allosteric properties. The NADH binding site of hexameric type II citrate synthases.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 NAI A T106 R109 H110 T111 M112 I113 H114 Y145 F162 R163 K167 T106 R109 H110 T111 M112 I113 H114 Y145 F162 R163 K167
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1nxg, PDBe:1nxg, PDBj:1nxg
PDBsum1nxg
PubMed12741811
UniProtP0ABH7|CISY_ECOLI Citrate synthase (Gene Name=gltA)

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