Structure of PDB 6njp Chain E Binding Site BS01

Receptor Information
>6njp Chain E (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 IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain6njp Chain E Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6njp Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.
Resolution3.29 Å
Binding residue
(original residue number in PDB)		G180 G182 K183 S184 T185 F355
Binding residue
(residue number reindexed from 1)		G146 G148 K149 S150 T151 F321
Annotation score5
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:6njp, PDBe:6njp, PDBj:6njp
PDBsum6njp
PubMed30733444
UniProtB7UMA6

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