MolNFT v1 · #255214 · protein
AlphaFold monomer V2.0 prediction for fimbrial protein myfa (P33406)
P33406: “AlphaFold monomer V2.0 prediction for fimbrial protein myfa (P33406)”. 1 pocket (best druggability 0.35). MolNFT v1 #255214 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P33406
- Type
- protein
- Length
- 159 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x301437AEb4a9d7100Ad0D7b67830522a5E0Ab5e9
- Molecule
- Fimbrial protein myfa
- UniProt
- P33406
- Pockets
- 1 · best druggability 0.35
Structure
1 distinct chain · 2% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fimbrial protein myfa | protein | 159 | 2% helix, 35% strand | P33406 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.35 | 0.76 | 17 | empty |
Compared structures
- 5LND · Crystal structure of self-complemented myfa, the major subunit of myf fimbriae from… · an experimental structure of the same protein · chain A against B, TM-score 0.69
- 5LO7 · Crystal structure of self-complemented myfa, the major subunit of myf fimbriae from… · an experimental structure of the same protein · chain A against B, TM-score 0.68
- 5LO7 · Crystal structure of self-complemented MyfA, the major subunit of Myf fimbriae from… · an experimental structure of the same protein · chain A against B, TM-score 0.68
- 5LN8 · Crystal structure of self-complemented MyfA, the major subunit of Myf fimbriae from… · an experimental structure of the same protein · chain A against B, TM-score 0.68
- 5LN8 · Crystal structure of self-complemented myfa, the major subunit of myf fimbriae from… · an experimental structure of the same protein · chain A against B, TM-score 0.68
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 P33406
- Elsewhere: UniProt P33406 · AlphaFold DB P33406
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