Structure of PDB 1ffg Chain C Binding Site BS01

Receptor Information
>1ffg Chain C (length=128) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGY
GFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQA
GASGYVVKPFTAATLEEKLNKIFEKLGM
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain1ffg Chain C Residue 130 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ffg Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		D13 D57 N59
Binding residue
(residue number reindexed from 1)		D12 D56 N58
Annotation score4
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000156 phosphorelay response regulator activity
GO:0000287 magnesium ion binding
GO:0005515 protein binding
GO:0016407 acetyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0000160 phosphorelay signal transduction system
GO:0006935 chemotaxis
GO:0007165 signal transduction
GO:0009454 aerotaxis
GO:0018393 internal peptidyl-lysine acetylation
GO:0043052 thermotaxis
GO:0050920 regulation of chemotaxis
GO:0071977 bacterial-type flagellum-dependent swimming motility
GO:0097588 archaeal or bacterial-type flagellum-dependent cell motility
GO:1902021 regulation of bacterial-type flagellum-dependent cell motility
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009288 bacterial-type flagellum
GO:0009433 bacterial-type flagellum basal body, C ring
GO:0120107 bacterial-type flagellum rotor complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ffg, PDBe:1ffg, PDBj:1ffg
PDBsum1ffg
PubMed11134926
UniProtP0AE67|CHEY_ECOLI Chemotaxis protein CheY (Gene Name=cheY)

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