Research workbench
AlphaFold monomer V2.0 prediction for phosphoenolpyruvate-protein phosphotransferase (P08839)
Analyse AlphaFold monomer V2.0 prediction for phosphoenolpyruvate-protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P08839
- Type
- protein
- Length
- 575 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- Phosphoenolpyruvate-protein phosphotransferase
- UniProt
- P08839
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoenolpyruvate-protein phosphotransferase | protein | 575 | 53% helix, 13% strand | P08839 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 709 | 0.75 | 0.80 | 89 | empty |
| 2 | 216 | 0.60 | 0.81 | 34 | empty |
| 3 | 110 | 0.53 | 0.83 | 25 | empty |
Compared structures
- 2N5T · Ensemble solution structure of the phosphoenolpyruvate-enzyme I complex from the… · an experimental structure of the same protein · chain A against A, TM-score 0.75
- 2N5T · Ensemble solution structure of the phosphoenolpyruvate-Enzyme I complex from the… · an experimental structure of the same protein · chain A against A, TM-score 0.75
- 2HWG · Structure of phosphorylated enzyme I of the PHOSPHOENOLPYRUVATE:SUGAR phosphotransferase… · an experimental structure of the same protein · chain A against A, TM-score 0.73
- 2HWG · Structure of phosphorylated Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase… · an experimental structure of the same protein · chain A against A, TM-score 0.73
- 2KX9 · Solution structure of the enzyme I dimer using residual dipolar couplings and small angle… · an experimental structure of the same protein · chain A against A, TM-score 0.65
- 2KX9 · Solution Structure of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle… · an experimental structure of the same protein · chain A against A, TM-score 0.65
- 2L5H · Solution structure of the H189Q mutant of the enzyme I dimer using residual dipolar… · an experimental structure of the same protein · chain A against A, TM-score 0.61
- 2L5H · Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar… · an experimental structure of the same protein · chain A against A, TM-score 0.61
- 2XDF · Solution structure of the enzyme I dimer complexed with hpr using residual dipolar… · an experimental structure of the same protein · chain A against A, TM-score 0.55
- 2XDF · Solution Structure of the Enzyme I Dimer Complexed with HPr Using Residual Dipolar… · an experimental structure of the same protein · chain A against A, TM-score 0.55
- 1EZD · Amino terminal domain of enzyme I from escherichia COLI NMR, 16 structures · an experimental structure of the same protein · chain A against A, TM-score 0.43
- 1EZD · Amino terminal domain of enzyme I from escherichia COLI NMR, 16 structures · an experimental structure of the same protein · chain A against A, TM-score 0.43
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 P08839
- Elsewhere: UniProt P08839 · AlphaFold DB P08839
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