Structure of PDB 5ybi Chain B Binding Site BS08
Receptor Information
>5ybi Chain B (length=345) Species:
623
(Shigella flexneri) [
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HMHTQVGRGLLGAVVNPLGEVTDKFAVTDNSEILYRPVDNAPPLYSERAA
IEKPFLTGIKVIDSLLTCGEGQRMGIFASAGCGKTFLMNMLIEHSGADIY
VIGLIGERGREVTETVDYLKNSEKKSRCVLVYATSDYSSVDRCNAAYIAT
AIAEFFRTEGHKVALFIDSLTRYARALRDVALAAGESPARRGYPVSVFDS
LPRLLERPGKLKAGGSITAFYTVLLEDDDFADPLAEEVRSILDGHIYLSR
NLAQKGQFPAIDSLKSISRVFTQVVDEKHRIMAAAFRELLSEIEELRTII
DKPGENASQDKIYNKISVVESFLKQDYRLGFTYEQTMELIGETIR
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
5ybi Chain B Residue 516 [
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Receptor-Ligand Complex Structure
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PDB
5ybi
Structural Insight Into Conformational Changes Induced by ATP Binding in a Type III Secretion-Associated ATPase FromShigella flexneri.
Resolution
2.268 Å
Binding residue
(original residue number in PDB)
T85 L99 G100
Binding residue
(residue number reindexed from 1)
T4 L18 G19
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
K165 E188 R189 R350
Catalytic site (residue number reindexed from 1)
K84 E107 R108 R269
Enzyme Commision number
7.4.2.8
: protein-secreting ATPase.
Gene Ontology
Molecular Function
GO:0005524
ATP binding
GO:0016887
ATP hydrolysis activity
Biological Process
GO:0009058
biosynthetic process
GO:0030254
protein secretion by the type III secretion system
Cellular Component
GO:0005737
cytoplasm
GO:0030257
type III protein secretion system complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:5ybi
,
PDBe:5ybi
,
PDBj:5ybi
PDBsum
5ybi
PubMed
30013545
UniProt
P0A1C1
|SCTN_SHIFL Type 3 secretion system ATPase (Gene Name=sctN)
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