Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase, muscle type (P00511)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P00511
- Type
- protein
- Length
- 780 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- ATP-dependent 6-phosphofructokinase, muscle type
- UniProt
- P00511
- Pockets
- 10 · best druggability 0.81
Structure
1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent 6-phosphofructokinase, muscle type | protein | 780 | 47% helix, 18% strand | P00511 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 532 | 0.81 | 0.87 | 60 | empty |
| 2 | 540 | 0.73 | 0.81 | 48 | empty |
| 3 | 230 | 0.67 | 0.84 | 37 | empty |
| 4 | 100 | 0.65 | 0.90 | 30 | empty |
| 5 | 179 | 0.53 | 0.79 | 25 | empty |
Compared structures
- 3O8N · Structure of phosphofructokinase from rabbit skeletal muscle · an experimental structure of the same protein · chain A against A, TM-score 0.95
- 3O8N · Structure of phosphofructokinase from rabbit skeletal muscle · an experimental structure of the same protein · chain A against A, TM-score 0.95
- 3O8L · Structure of phosphofructokinase from rabbit skeletal muscle · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 3O8L · Structure of phosphofructokinase from rabbit skeletal muscle · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 P00511
- Elsewhere: UniProt P00511 · AlphaFold DB P00511
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