Research workbench
MOUSE SOD1
Analyse MOUSE SOD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GTT
- Type
- protein
- Length
- 918 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- P08228
- Ligands
- ZN
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 153 | 6% helix, 41% strand | P08228 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1078 | 0.78 | 0.80 | 99 | empty |
| 2 | 157 | 0.67 | 0.88 | 28 | empty |
| 3 | 174 | 0.65 | 0.86 | 29 | empty |
| 4 | 157 | 0.64 | 0.86 | 34 | empty |
| 5 | 161 | 0.42 | 0.73 | 27 | empty |
Interfaces
6 interfaces between chains.
- A–B · 752 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 750 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 734 Ų buried · 5 hydrogen bonds · protein-protein
- A–E · 330 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 294 Ų buried · 5 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 P08228
- Elsewhere: RCSB PDB 3GTT · PDBe 3GTT · UniProt P08228
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