MolNFT v1 · #17644 · protein
Crystal structure of familial als mutant S134N of human CU,ZN superoxide dismutase (cuznsod) to 1.3A resolution
1OZU · Superoxide dismutase [cu-zn]: “Crystal structure of familial als mutant S134N of human CU,ZN superoxide dismutase (cuznsod) to 1.3A…”. X-ray diffraction, 2 ligands (ZN, SO4), 1 pocket (best druggability 0.59). MolNFT v1 #17644 on…
- PDB
- 1OZU
- Type
- protein
- Length
- 277 residues
- Chains
- 2
- 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
- 1 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 150 | 3% helix, 41% strand | P00441 |
| B | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 127 | 3% helix, 47% strand | P00441 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 231 | 0.59 | 0.80 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 667 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, oxidation).
Compared structures
- 1OZU · Crystal Structure of Familial ALS Mutant S134N of human 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 1OZU · PDBe 1OZU · UniProt P00441
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