Structure of PDB 1fqw Chain A Binding Site BS02
Receptor Information
>1fqw Chain A (length=128) Species:
562
(Escherichia coli) [
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ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGY
GFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQA
GASGYVVKPFTAATLEEKLNKIFEKLGM
Ligand information
Ligand ID
BEF
InChI
InChI=1S/Be.3FH/h;3*1H/q+2;;;/p-3
InChIKey
OGIAHMCCNXDTIE-UHFFFAOYSA-K
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
[Be-](F)(F)F
ACDLabs 10.04
CACTVS 3.341
F[Be-](F)F
Formula
Be F3
Name
BERYLLIUM TRIFLUORIDE ION
ChEMBL
DrugBank
ZINC
PDB chain
1fqw Chain A Residue 130 [
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Receptor-Ligand Complex Structure
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PDB
1fqw
Crystal structure of activated CheY. Comparison with other activated receiver domains.
Resolution
2.37 Å
Binding residue
(original residue number in PDB)
D57 W58 N59 T87 A88 K109
Binding residue
(residue number reindexed from 1)
D56 W57 N58 T86 A87 K108
Annotation score
1
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:1fqw
,
PDBe:1fqw
,
PDBj:1fqw
PDBsum
1fqw
PubMed
11279165
UniProt
P0AE67
|CHEY_ECOLI Chemotaxis protein CheY (Gene Name=cheY)
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