Research workbench
Flgg structure based on the cryoem MAP of the bacterial flagellar polyrod
Analyse Flgg structure based on the cryoem MAP of the bacterial flagellar polyrod in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WRH
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A1J3
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 186 | — | P0A1J3 |
Compared structures
- 5WRH · FlgG structure based on the CryoEM map of the bacterial flagellar polyrod · the same entry in another collection · chain A against A, TM-score 1.00
- P0A1J3 · AlphaFold monomer V2.0 prediction for flagellar basal-body rod protein flgg (P0A1J3) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P0A1J3
- Elsewhere: RCSB PDB 5WRH · PDBe 5WRH · UniProt P0A1J3
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