Research workbench
Heterodimers of fals mutant sod enzyme
Analyse Heterodimers of fals mutant sod enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DTK
- Type
- protein
- Length
- 1,562 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase C111S/D83S-C111S heterodimer
- EC
- 1.15.1.1
- UniProt
- P00441
- Ligands
- ZN, CU
- Pockets
- 10 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase C111S/D83S-C111S heterodimer (EC 1.15.1.1) | protein | 312 | 5% helix, 38% strand | P00441 |
| C | Superoxide dismutase C111S/D83S-C111S heterodimer (EC 1.15.1.1) | protein | 311 | 5% helix, 39% strand | P00441 |
| E, G, I | Superoxide dismutase C111S/D83S-C111S heterodimer (EC 1.15.1.1) | protein | 313 | 7% helix, 39% strand | P00441 |
Ligands and binding sites
- ZN · Zinc ion · metal · 10 copies · chains A, C, E, G, I
- CU · Copper (II) ion · metal · 10 copies · chains A, C, E, G, I
- MLI · Malonate ion · additive · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 772 | 0.76 | 0.81 | 92 | empty |
| 2 | 682 | 0.68 | 0.77 | 87 | empty |
| 3 | 343 | 0.62 | 0.78 | 49 | empty |
| 4 | 215 | 0.62 | 0.82 | 27 | empty |
| 5 | 346 | 0.62 | 0.78 | 38 | empty |
Interfaces
5 interfaces between chains.
- C–I · 757 Ų buried · 10 hydrogen bonds · protein-protein
- G–I · 733 Ų buried · 17 hydrogen bonds · protein-protein
- E–G · 394 Ų buried · 7 hydrogen bonds · protein-protein
- A–G · 344 Ų buried · 4 hydrogen bonds · protein-protein
- C–E · 47 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 6DTK · Heterodimers of FALS mutant SOD enzyme · the same entry in another collection · chain I against I, 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 P00441
- Elsewhere: RCSB PDB 6DTK · PDBe 6DTK · UniProt P00441
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