Research workbench
Superoxide dismutase with manganese from deinococcus radiodurans
Analyse Superoxide dismutase with manganese from deinococcus radiodurans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AW9
- Type
- protein
- Length
- 418 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [mn]
- EC
- 1.15.1.1
- UniProt
- Q9RUV2
- Ligands
- MN
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [mn] (EC 1.15.1.1) | protein | 210 | 51% helix, 12% strand | Q9RUV2 |
| B | Superoxide dismutase [mn] (EC 1.15.1.1) | protein | 208 | 53% helix, 12% strand | Q9RUV2 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.57 | 0.80 | 23 | empty |
| 2 | 186 | 0.53 | 0.78 | 20 | empty |
| 3 | 89 | 0.41 | 0.77 | 22 | empty |
| 4 | 92 | 0.40 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 937 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2AW9 · Superoxide dismutase with manganese from Deinococcus radiodurans · the same entry in another collection · chain A against A, TM-score 1.00
- Q9RUV2 · AlphaFold monomer V2.0 prediction for superoxide dismutase [mn] (Q9RUV2) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9RUV2
- Elsewhere: RCSB PDB 2AW9 · PDBe 2AW9 · UniProt Q9RUV2
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