Research workbench
Nickel superoxide dismutase (nisod) cn-treated apo structure
Analyse Nickel superoxide dismutase (nisod) cn-treated apo structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T6Q
- Type
- protein
- Length
- 332 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [ni]
- EC
- 1.15.1.1
- UniProt
- P80735
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Superoxide dismutase [ni] (EC 1.15.1.1) | protein | 110 | 81% helix, 0% strand | P80735 |
| B | Superoxide dismutase [ni] (EC 1.15.1.1) | protein | 112 | 81% helix, 0% strand | P80735 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.37 | 0.76 | 22 | empty |
| 2 | 89 | 0.34 | 0.74 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 346 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 326 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 323 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 P80735
- Elsewhere: RCSB PDB 1T6Q · PDBe 1T6Q · UniProt P80735
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