Research workbench
Recognition and targeting mechanisms by chaperones in flagella assembly and operation
Analyse Recognition and targeting mechanisms by chaperones in flagella assembly and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KP0
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar protein FLIT,FLAGELLUM-specific ATP synthase
- EC
- 3.6.3.14
- UniProt
- P0A1N2, P26465
Structure
solution nmr · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar protein FLIT,FLAGELLUM-specific ATP synthase (EC 3.6.3.14) | protein | 140 | 74% helix, 0% strand | P0A1N2, P26465 |
Compared structures
- 5KP0 · Recognition and targeting mechanisms by chaperones in flagella assembly and operation · the same entry in another collection · chain A against A, TM-score 1.00
- P0A1N2 · AlphaFold monomer V2.0 prediction for flagellar protein flit (P0A1N2) · a predicted model of the same protein · chain A against A, TM-score 0.59
- P26465 · AlphaFold monomer V2.0 prediction for flagellum-specific ATP synthase (P26465) · a predicted model of the same protein · chain A against A, TM-score 0.42
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 P0A1N2
- Every structure of UniProt P26465
- Elsewhere: RCSB PDB 5KP0 · PDBe 5KP0 · UniProt P0A1N2 · UniProt P26465
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