Research workbench
C.elegans MnSOD-3 mutant - Q142H
Analyse C.elegans MnSOD-3 mutant - Q142H in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ELK
- Type
- protein
- Length
- 388 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.65
- Source
- Caenorhabditis elegans
- Molecule
- Superoxide dismutase [Mn] 2, mitochondrial
- EC
- 1.15.1.1
- UniProt
- P41977
- Ligands
- MN, SO4
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · resolution 1.65 · 1 distinct chain · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Superoxide dismutase [Mn] 2, mitochondrial (EC 1.15.1.1) | protein | 194 | 57% helix, 13% strand | P41977 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, C
- SO4 · Sulfate ion · ion · 6 copies · chains A, C
- GOL · Glycerol · additive · chains C
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 | 136 | 0.49 | 0.78 | 26 | SO4 |
Interfaces
1 interface between chains.
- A–C · 914 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
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 P41977
- Elsewhere: RCSB PDB 6ELK · PDBe 6ELK · UniProt P41977
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.