Research workbench
The crystal structure of the eukaryotic fesod from vigna unguiculata suggests a new enzymatic mechanism
Analyse The crystal structure of the eukaryotic fesod from vigna unguiculata suggests a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UNF
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- Q9M7R2
- Ligands
- FE
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Iron superoxide dismutase (EC 1.15.1.1) | protein | 214 | 54% helix, 12% strand | Q9M7R2 |
Ligands and binding sites
- FE · Fe (III) ion · metal · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.28 | 0.74 | 15 | empty |
Compared structures
- 1UNF · The crystal structure of the eukaryotic FeSOD from Vigna unguiculata suggests a new… · the same entry in another collection · chain X against X, TM-score 1.00
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 Q9M7R2
- Elsewhere: RCSB PDB 1UNF · PDBe 1UNF · UniProt Q9M7R2
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