Research workbench
AlphaFold monomer V2.0 prediction for protochlorophyllide reductase B, chloroplastic (P21218)
Analyse AlphaFold monomer V2.0 prediction for protochlorophyllide reductase B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P21218
- Type
- protein
- Length
- 401 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x28e51F615E58598362D09182b4f56f5cAD52f49a
- Molecule
- Protochlorophyllide reductase B, chloroplastic
- UniProt
- P21218
- Pockets
- 1 · best druggability 0.76
Structure
1 distinct chain · 36% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protochlorophyllide reductase B, chloroplastic | protein | 401 | 36% helix, 11% strand | P21218 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 555 | 0.76 | 0.83 | 70 | empty |
Compared structures
- 7JK9 · Helical filaments of plant light-dependent protochlorophyllide oxidoreductase (LPOR)… · an experimental structure of the same protein · chain A against DA, TM-score 0.78
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 P21218
- Elsewhere: UniProt P21218 · AlphaFold DB P21218
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