Research workbench
AlphaFold monomer V2.0 prediction for ferrochelatase (Q5N2B2)
Analyse AlphaFold monomer V2.0 prediction for ferrochelatase (Q5N2B2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5N2B2
- Type
- protein
- Length
- 387 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Ferrochelatase
- UniProt
- Q5N2B2
- Pockets
- 4 · best druggability 0.82
Structure
1 distinct chain · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferrochelatase | protein | 387 | 51% helix, 13% strand | Q5N2B2 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.82 | 0.83 | 80 | empty |
| 2 | 92 | 0.45 | 0.80 | 15 | empty |
| 3 | 62 | 0.27 | 0.73 | 14 | empty |
| 4 | 51 | 0.25 | 0.73 | 12 | 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 Q5N2B2
- Elsewhere: UniProt Q5N2B2 · AlphaFold DB Q5N2B2
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