Research workbench
AlphaFold monomer V2.0 prediction for fimbrial protein (Q53391)
Analyse AlphaFold monomer V2.0 prediction for fimbrial protein (Q53391) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q53391
- Type
- protein
- Length
- 23 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC0491A7e4a5851164cEffD648c5067B32B6C2422
- UniProt
- Q53391
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 23 | — | Q53391 |
Compared structures
- 1KB8 · A comparison of NMR solution structures of the receptor binding domains of pseudomonas… · an experimental structure of the same protein · chain A against A, TM-score 0.24
- 1KB8 · A comparison of NMR solution structures of the receptor binding domains of pseudomonas… · an experimental structure of the same protein · chain A against A, TM-score 0.24
- 1KB7 · A comparison of NMR solution structures of the receptor binding domains of pseudomonas… · an experimental structure of the same protein · chain A against A, TM-score 0.19
- 1KB7 · A comparison of NMR solution structures of the receptor binding domains of pseudomonas… · an experimental structure of the same protein · chain A against A, TM-score 0.19
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 Q53391
- Elsewhere: UniProt Q53391 · AlphaFold DB Q53391
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