Research workbench
Human CYS57/156ALA superoxide dismutase-1 (SOD1), as isolated.
Analyse Human CYS57/156ALA superoxide dismutase-1 (SOD1), as isolated. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FOI
- Type
- protein
- Length
- 1,835 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- P00441
- Ligands
- ZN, SO4
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F, D, G, I, K, M, O, Q, S, U | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 153 | 6% helix, 41% strand | P00441 |
| W | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 152 | 2% helix, 41% strand | P00441 |
Ligands and binding sites
- ZN · Zinc ion · metal · 12 copies · chains A, F, D, G, I, K, M, O, Q, S, U, W
- SO4 · Sulfate ion · ion · 13 copies · chains A, F, K, M, D, G, I, Q, W, S, U
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1057 | 0.78 | 0.80 | 108 | SO4 |
| 2 | 1054 | 0.78 | 0.80 | 106 | SO4 |
| 3 | 160 | 0.64 | 0.86 | 27 | empty |
| 4 | 478 | 0.64 | 0.77 | 42 | empty |
| 5 | 368 | 0.63 | 0.79 | 40 | empty |
Interfaces
18 interfaces between chains.
- M–O · 718 Ų buried · 4 hydrogen bonds · protein-protein
- I–K · 713 Ų buried · 4 hydrogen bonds · protein-protein
- A–F · 709 Ų buried · 4 hydrogen bonds · protein-protein
- D–G · 706 Ų buried · 4 hydrogen bonds · protein-protein
- Q–S · 700 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6FOI · Human Cys57/156Ala superoxide dismutase-1 (SOD1), as isolated. · the same entry in another collection · chain A against A, 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 6FOI · PDBe 6FOI · UniProt P00441
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