Research workbench
AlphaFold monomer V2.0 prediction for photosystem II CP47 reaction center protein (P27200)
Analyse AlphaFold monomer V2.0 prediction for photosystem II CP47 reaction center… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27200
- Type
- protein
- Length
- 514 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Photosystem II CP47 reaction center protein
- UniProt
- P27200
- Pockets
- 10 · best druggability 0.57
Structure
1 distinct chain · 49% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Photosystem II CP47 reaction center protein | protein | 514 | 49% helix, 10% strand | P27200 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 416 | 0.57 | 0.74 | 43 | empty |
| 2 | 155 | 0.55 | 0.81 | 23 | empty |
| 3 | 244 | 0.51 | 0.75 | 36 | empty |
| 4 | 52 | 0.51 | 0.87 | 24 | empty |
| 5 | 128 | 0.45 | 0.77 | 23 | empty |
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 P27200
- Elsewhere: UniProt P27200 · AlphaFold DB P27200
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