Structure of PDB 6njo Chain C Binding Site BS03

Receptor Information
>6njo Chain C (length=412) Species: 574521 (Escherichia coli O127:H6 str. E2348/69) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EGKIINIGGTIIKARLPKARIGAFYKIEPSQRLAEVIAIDEDEVFLLPFE
HVSGMYCGQWLSYQGDEFKIRVGDALLGRLIDGIGRPMESNIVAPYLPFE
RSLYAEPPDPLLRQVIDQPFILGVRAIDGLLTCGIGQRIGIFAGSGVGKS
TLLGMICNGASADIIVLALIGERGREVNEFLALLPQSTLSKCVLVVTTSD
RPALERMKAAFTATTIAEYFRDQGKNVLLMMDSVTRYARAARDVGLASGE
PDVRGGFPPSVFSSLPKLLERAGPAPKGSITAIYTVLLESDNVNDPIGDE
VRSILDGHIVLTRELAEENHFPAIDIGLSASRVMHNVVTSEHLRAAAECK
KLIATYKNVELLIRIGEYTMGQDPEADKAIKNRKLIQNFIQQSTKDISSY
EKTIESLFKVVA
Ligand information
Ligand IDAF3
InChIInChI=1S/Al.3FH/h;3*1H/q+3;;;/p-3
InChIKeyKLZUFWVZNOTSEM-UHFFFAOYSA-K
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		F[Al](F)F
FormulaAl F3
NameALUMINUM FLUORIDE
ChEMBL
DrugBank
ZINC
PDB chain6njo Chain D Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6njo Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.
Resolution3.34 Å
Binding residue
(original residue number in PDB)		S337 R366
Binding residue
(residue number reindexed from 1)		S303 R332
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K183 E206 R207 R366
Catalytic site (residue number reindexed from 1) K149 E172 R173 R332
Enzyme Commision number 7.4.2.8: protein-secreting ATPase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0009058 biosynthetic process
GO:0015031 protein transport
GO:0015986 proton motive force-driven ATP synthesis
GO:0030254 protein secretion by the type III secretion system
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005737 cytoplasm
GO:0030257 type III protein secretion system complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6njo, PDBe:6njo, PDBj:6njo
PDBsum6njo
PubMed30733444
UniProtB7UMA6

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