Structure of PDB 6njo Chain D

Receptor sequence
>6njoD (length=413) Species: 574521 (Escherichia coli O127:H6 str. E2348/69) [Search protein sequence]
YEGKIINIGGTIIKARLPKARIGAFYKIEPSQRLAEVIAIDEDEVFLLPF
EHVSGMYCGQWLSYQGDEFKIRVGDALLGRLIDGIGRPMESNIVAPYLPF
ERSLYAEPPDPLLRQVIDQPFILGVRAIDGLLTCGIGQRIGIFAGSGVGK
STLLGMICNGASADIIVLALIGERGREVNEFLALLPQSTLSKCVLVVTTS
DRPALERMKAAFTATTIAEYFRDQGKNVLLMMDSVTRYARAARDVGLASG
EPDVRGGFPPSVFSSLPKLLERAGPAPKGSITAIYTVLLESDNVNDPIGD
EVRSILDGHIVLTRELAEENHFPAIDIGLSASRVMHNVVTSEHLRAAAEC
KKLIATYKNVELLIRIGEYTMGQDPEADKAIKNRKLIQNFIQQSTKDISS
YEKTIESLFKVVA
3D structure
PDB6njo Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.
ChainD
Resolution3.34 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K183 E206 R207 R366
Catalytic site (residue number reindexed from 1) K150 E173 R174 R333
Enzyme Commision number 7.4.2.8: protein-secreting ATPase.
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 ADP D G180 V181 K183 S184 T185 F355 T428 G147 V148 K150 S151 T152 F322 T395
BS02 MG D S184 E206 S151 E173
BS03 AF3 D K183 E206 L321 K150 E173 L288
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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