MolNFT v1 · #126362 · protein
AlphaFold monomer V2.0 prediction for chaperone protein faee (P25401)
P25401: “AlphaFold monomer V2.0 prediction for chaperone protein faee (P25401)”. MolNFT v1 #126362 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P25401
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA2ED127c7DF83E1D9Fa8D7c517410A1D4A5B70F5
- UniProt
- P25401
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 258 | — | P25401 |
Compared structures
- 3GFU · FaeE-FaeG chaperone-major pilin complex of F4 ac 5/95 fimbriae · an experimental structure of the same protein · chain A against A, TM-score 0.82
- 3GFU · Faee-faeg chaperone-major pilin complex of F4 ac 5/95 fimbriae · an experimental structure of the same protein · chain A against A, TM-score 0.82
- 3GEW · FaeE-FaeG chaperone-major pilin complex of F4 ad fimbriae · an experimental structure of the same protein · chain A against C, TM-score 0.80
- 3GEW · Faee-faeg chaperone-major pilin complex of F4 ad fimbriae · an experimental structure of the same protein · chain A against C, TM-score 0.80
- 3F65 · The F4 fimbrial chaperone faee does not self-cap its interactive surfaces · an experimental structure of the same protein · chain A against A, TM-score 0.77
- 3F65 · The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces · an experimental structure of the same protein · chain A against A, TM-score 0.77
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 P25401
- Elsewhere: UniProt P25401 · AlphaFold DB P25401
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