Research workbench
Solution structure of the C-terminal domain of the flik
Analyse Solution structure of the C-terminal domain of the flik in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RRL
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar hook-length control protein
- UniProt
- P26416
Structure
solution nmr · 1 distinct chain · 22% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar hook-length control protein | protein | 169 | 22% helix, 16% strand | P26416 |
Compared structures
- 2RRL · Solution structure of the C-terminal domain of the FliK · the same entry in another collection · chain A against A, TM-score 1.00
- P26416 · AlphaFold monomer V2.0 prediction for flagellar hook-length control protein (P26416) · a predicted model of the same protein · chain A against A, TM-score 0.55
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 P26416
- Elsewhere: RCSB PDB 2RRL · PDBe 2RRL · UniProt P26416
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