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Flagellar export chaperone in complex with its cognate binding partner

Analyse Flagellar export chaperone in complex with its cognate binding partner in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ORY
Type
protein
Length
159 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.45
Source
Aquifex aeolicus
Molecule
flagellar protein FliS; Flagellin
UniProt
O67806, O67803
Ligands
PO4

Structure

x-ray diffraction · resolution 2.45 · 2 distinct chains · 82% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Aflagellar protein FliSprotein11983% helix, 0% strandO67806
BFlagellinprotein4080% helix, 0% strandO67803

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 1943 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 1ORY · Flagellar export chaperone in complex with its cognate binding partner · the same entry in another collection · chain A against A, TM-score 1.00
  • O67803 · AlphaFold monomer V2.0 prediction for flagellin (O67803) · a predicted model of the same protein · chain B against A, TM-score 0.41

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