Research workbench
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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | flagellar protein FliS | protein | 119 | 83% helix, 0% strand | O67806 |
| B | Flagellin | protein | 40 | 80% helix, 0% strand | O67803 |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O67806
- Every structure of UniProt O67803
- Elsewhere: RCSB PDB 1ORY · PDBe 1ORY · UniProt O67806 · UniProt O67803
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