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The 1.6 a structure of fe-superoxide dismutase from the thermophilic cyanobacterium thermosynechococcus elongatus : correlation of epr and structural characteristics
Analyse The 1.6 a structure of fe-superoxide dismutase from the thermophilic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MY6
- Type
- protein
- Length
- 396 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iron (III) superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- Q8DIR2
- Ligands
- FE
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Iron (III) superoxide dismutase (EC 1.15.1.1) | protein | 198 | 57% helix, 13% strand | Q8DIR2 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 230 | 0.54 | 0.77 | 21 | empty |
| 2 | 226 | 0.54 | 0.77 | 24 | empty |
| 3 | 53 | 0.29 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 942 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1MY6 · The 1.6 A Structure of Fe-Superoxide Dismutase from the thermophilic cyanobacterium… · the same entry in another collection · chain A against A, 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 Q8DIR2
- Elsewhere: RCSB PDB 1MY6 · PDBe 1MY6 · UniProt Q8DIR2
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