MolNFT v1 · #318457 · protein
AlphaFold monomer V2.0 prediction for pts system glucose-specific eiicba component (P20166)
P20166: “AlphaFold monomer V2.0 prediction for pts system glucose-specific eiicba component (P20166)”. 9 pockets (best druggability 0.72). MolNFT v1 #318457 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P20166
- Type
- protein
- Length
- 699 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa130963659F9ADED1C735201Bb05F57675e205B8
- Molecule
- Pts system glucose-specific eiicba component
- UniProt
- P20166
- Pockets
- 9 · best druggability 0.72
Structure
1 distinct chain · 55% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pts system glucose-specific eiicba component | protein | 699 | 55% helix, 14% strand | P20166 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 564 | 0.72 | 0.80 | 50 | empty |
| 2 | 137 | 0.52 | 0.80 | 19 | empty |
| 3 | 213 | 0.51 | 0.76 | 28 | empty |
| 4 | 67 | 0.48 | 0.83 | 18 | empty |
| 5 | 143 | 0.46 | 0.77 | 18 | empty |
Compared structures
- 1GPR · Refined crystal structure of iia domain of the glucose permease of bacillus subtilis at… · an experimental structure of the same protein · chain A against A, TM-score 0.22
- 1GPR · Refined crystal structure of iia domain of the glucose permease of bacillus subtilis at… · an experimental structure of the same protein · chain A against A, TM-score 0.22
- 1AX3 · Solution NMR structure of B. subtilis iiaglc, 16 structures · an experimental structure of the same protein · chain A against A, TM-score 0.21
- 1AX3 · Solution NMR structure of B. subtilis iiaglc, 16 structures · an experimental structure of the same protein · chain A against A, TM-score 0.21
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 P20166
- Elsewhere: UniProt P20166 · AlphaFold DB P20166
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