Research workbench
Elongated conformer of the human copper chaperone for SOD1 complexed with human SOD1
Analyse Elongated conformer of the human copper chaperone for SOD1 complexed with human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FON
- Type
- protein
- Length
- 810 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper chaperone for superoxide dismutase; Superoxide dismutase [cu-zn]
- EC
- 1.15.1.1
- UniProt
- O14618, P00441
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Copper chaperone for superoxide dismutase | protein | 252 | 12% helix, 41% strand | O14618 |
| B, D | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 153 | 5% helix, 41% strand | P00441 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.57 | 0.76 | 39 | empty |
| 2 | 358 | 0.57 | 0.75 | 42 | empty |
| 3 | 171 | 0.55 | 0.80 | 24 | empty |
| 4 | 202 | 0.54 | 0.79 | 29 | empty |
| 5 | 125 | 0.41 | 0.76 | 25 | empty |
Interfaces
3 interfaces between chains.
- C–D · 778 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 778 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 229 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6FON · Elongated conformer of the human copper chaperone for SOD1 complexed with human SOD1 · the same entry in another collection · chain A against A, TM-score 1.00
- O14618 · AlphaFold monomer V2.0 prediction for copper chaperone for superoxide dismutase (O14618) · a predicted model of the same protein · chain A against A, TM-score 0.62
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 O14618
- Every structure of UniProt P00441
- Elsewhere: RCSB PDB 6FON · PDBe 6FON · UniProt O14618 · UniProt P00441
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.