MolNFT v1 · #18592 · protein
Structure of human CU,ZN superoxide dismutase
1PU0 · Superoxide dismutase [cu-zn]: “Structure of human CU,ZN superoxide dismutase”. X-ray diffraction, 3 ligands (CU1, ZN, SO4), 17 pockets (best druggability 0.79). MolNFT v1 #18592 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1PU0
- Type
- protein
- Length
- 1,530 residues
- Chains
- 10
- 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
- CU1, ZN, SO4
- Pockets
- 17 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 153 | 6% helix, 39% strand | P00441 |
Ligands and binding sites
- CU1 · Copper (I) ion · metal · 10 copies · chains A, B, C, D, E, F, G, H, I, J
- ZN · Zinc ion · metal · 10 copies · chains A, B, C, D, E, F, G, H, I, J
- SO4 · Sulfate ion · ion · 3 copies · chains B, D, F, H, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 935 | 0.79 | 0.81 | 87 | empty |
| 2 | 836 | 0.72 | 0.77 | 92 | empty |
| 3 | 699 | 0.72 | 0.78 | 77 | SO4 |
| 4 | 179 | 0.67 | 0.87 | 31 | empty |
| 5 | 186 | 0.64 | 0.84 | 38 | empty |
Interfaces
13 interfaces between chains.
- A–B · 740 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 731 Ų buried · 5 hydrogen bonds · protein-protein
- I–J · 720 Ų buried · 4 hydrogen bonds · protein-protein
- G–H · 720 Ų buried · 4 hydrogen bonds · protein-protein
- E–F · 711 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 1PU0 · Structure 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 1PU0 · PDBe 1PU0 · UniProt P00441
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.