Research workbench
Domain II of the human copper chaperone in complex with human CU,ZN superoxide dismutase
Analyse Domain II of the human copper chaperone in complex with human 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
- 6FOL
- Type
- protein
- Length
- 1,206 residues
- Chains
- 8
- 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
- 18 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 4% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, H | Copper chaperone for superoxide dismutase | protein | 148 | 5% helix, 43% strand | O14618 |
| B, C, F, G | Superoxide dismutase [cu-zn] (EC 1.15.1.1) | protein | 153 | 5% helix, 41% strand | P00441 |
| E | Copper chaperone for superoxide dismutase | protein | 150 | 3% helix, 41% strand | O14618 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
- PE8 · 3,6,9,12,15,18,21-heptaoxatricosane-1,23-diol · additive · 2 copies · chains C, D, A, B
- GOL · Glycerol · additive · chains F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 238 | 0.73 | 0.88 | 43 | empty |
| 2 | 249 | 0.72 | 0.87 | 41 | empty |
| 3 | 196 | 0.72 | 0.89 | 31 | empty |
| 4 | 206 | 0.67 | 0.85 | 37 | empty |
| 5 | 386 | 0.59 | 0.76 | 52 | empty |
Interfaces
12 interfaces between chains.
- E–F · 699 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 697 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 695 Ų buried · 10 hydrogen bonds · protein-protein
- G–H · 682 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 467 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6FOL · Domain II of the human copper chaperone in complex with human Cu,Zn superoxide dismutase · the same entry in another collection · chain H against H, 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 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 O14618
- Every structure of UniProt P00441
- Elsewhere: RCSB PDB 6FOL · PDBe 6FOL · UniProt O14618 · UniProt P00441
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