Structure of PDB 4jae Chain B

Receptor sequence
>4jaeB (length=426) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
ADTKAKLTLDGDTAVELDVLKGTLGQDVIDIRTLGSKGVFTFDPGFTSTT
SCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQY
DEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLD
VNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNM
MFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFA
CIAAGIASLWGPAHGGANEAALKMLEEIGKKENIPEFVRRAKDKNDSFRL
MGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELENIALNDP
YFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHS
DGMKIARPRQLYTGYEKRDFKSDIKR
3D structure
PDB4jae Enzyme-substrate complexes of allosteric citrate synthase: Evidence for a novel intermediate in substrate binding.
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S1234 H1264 H1305 R1314 D1362
Catalytic site (residue number reindexed from 1) S234 H264 H305 R314 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 B T1106 R1109 H1110 T1111 M1112 Y1145 I1159 F1162 R1163 K1167 N1189 T106 R109 H110 T111 M112 Y145 I159 F162 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4jae, PDBe:4jae, PDBj:4jae
PDBsum4jae
PubMed23954305
UniProtP0ABH7|CISY_ECOLI Citrate synthase (Gene Name=gltA)

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