Structure of PDB 1mih Chain A Binding Site BS02

Receptor Information
>1mih Chain A (length=128) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGY
GFVISDWRMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQA
GASGYVVKPFTAATLEEKLNKIFEKLGM
Ligand information
Ligand IDBEF
InChIInChI=1S/Be.3FH/h;3*1H/q+2;;;/p-3
InChIKeyOGIAHMCCNXDTIE-UHFFFAOYSA-K
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[Be-](F)(F)F
ACDLabs 10.04
CACTVS 3.341
F[Be-](F)F
FormulaBe F3
NameBERYLLIUM TRIFLUORIDE ION
ChEMBL
DrugBank
ZINC
PDB chain1mih Chain A Residue 130 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1mih CheZ-mediated dephosphorylation of the Escherichia coli chemotaxis response regulator CheY: role for CheY glutamate 89.
Resolution2.7 Å
Binding residue
(original residue number in PDB)
D57 W58 R59 T87 K109
Binding residue
(residue number reindexed from 1)
D56 W57 R58 T86 K108
Annotation score1
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:1mih, PDBe:1mih, PDBj:1mih
PDBsum1mih
PubMed12591865
UniProtP0AE67|CHEY_ECOLI Chemotaxis protein CheY (Gene Name=cheY)

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