Research workbench
Crystal structure of fals-associated human copper-zinc superoxide dismutase (cuznsod) mutant D125H to 1.4A
Analyse Crystal structure of fals-associated human copper-zinc superoxide dismutase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P1V
- Type
- protein
- Length
- 436 residues
- Chains
- 3
- 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
- 2 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 146 | 4% helix, 41% strand | P00441 |
| B | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 144 | 3% helix, 44% strand | P00441 |
Ligands and binding sites
- ZN · Zinc ion · metal · 6 copies · chains A, B, C
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
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 | 205 | 0.61 | 0.82 | 29 | empty |
| 2 | 70 | 0.32 | 0.75 | 21 | empty |
Interfaces
2 interfaces between chains.
- A–B · 704 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 12 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 3 modified (disulfide, oxidation).
Compared structures
- 1P1V · Crystal Structure of FALS-associated human Copper-Zinc Superoxide Dismutase (CuZnSOD)… · 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 1P1V · PDBe 1P1V · UniProt P00441
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