Research workbench
AlphaFold monomer V2.0 prediction for minor fimbrium subunit MFA5 (B2RHG5)
Analyse AlphaFold monomer V2.0 prediction for minor fimbrium subunit MFA5 (B2RHG5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2RHG5
- Type
- protein
- Length
- 1,228 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- UniProt
- B2RHG5
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1228 | — | B2RHG5 |
Compared structures
- 6TO1 · Crystal structure of three N-terminal domains of the type V pili tip protein MFA5 from… · an experimental structure of the same protein · chain A against A, TM-score 0.44
- 6TO1 · Crystal structure of three N-terminal domains of the type V pili tip protein Mfa5 from… · an experimental structure of the same protein · chain A against A, TM-score 0.44
- 6TNJ · Crystal structure of the vwf domain of the type V pili tip protein MFA5 from… · an experimental structure of the same protein · chain A against A, TM-score 0.23
- 6TNJ · Crystal structure of the vWF domain of the type V pili tip protein Mfa5 from… · an experimental structure of the same protein · chain A against A, TM-score 0.23
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 B2RHG5
- Elsewhere: UniProt B2RHG5 · AlphaFold DB B2RHG5
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