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AlphaFold monomer V2.0 prediction for chlorophyll a-B binding protein CP24 10B, chloroplastic (P27525)
Analyse AlphaFold monomer V2.0 prediction for chlorophyll a-B binding protein CP24 10B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P27525
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0F7aAe0F58509eB3BaA013d642d748C7C38B0F93
- Molecule
- Chlorophyll a-B binding protein CP24 10B, chloroplastic
- UniProt
- P27525
- Pockets
- 3 · best druggability 0.64
Structure
1 distinct chain · 42% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chlorophyll a-B binding protein CP24 10B, chloroplastic | protein | 256 | 42% helix, 3% strand | P27525 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.64 | 0.80 | 38 | empty |
| 2 | 305 | 0.61 | 0.78 | 37 | empty |
| 3 | 72 | 0.29 | 0.73 | 15 | 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 P27525
- Elsewhere: UniProt P27525 · AlphaFold DB P27525
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