Research workbench
Amyotrophic lateral sclerosis and structural defects in CU,ZN superoxide dismutase
Analyse Amyotrophic lateral sclerosis and structural defects in CU,ZN superoxide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SPD
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide dismutase
- EC
- 1.15.1.1
- UniProt
- P00441
- Ligands
- ACE, CU, ZN
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Superoxide dismutase (EC 1.15.1.1) | protein | 153 | 6% helix, 31% strand | P00441 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, B
- CU · Copper (II) ion · metal · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 248 | 0.58 | 0.79 | 30 | empty |
| 2 | 118 | 0.39 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 661 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 2 disulfide (covalent ligand, disulfide).
Compared structures
- 1SPD · Amyotrophic lateral sclerosis and structural defects in CU,ZN superoxide dismutase · 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 1SPD · PDBe 1SPD · UniProt P00441
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