MolNFT v1 · #149048 · protein
Domain II of the human copper chaperone in complex with human CU,ZN superoxide dismutase
6FOL · Copper chaperone for superoxide dismutase: “Domain II of the human copper chaperone in complex with human CU,ZN superoxide dismutase”. X-ray diffraction, 1 ligand (ZN), 18 pockets (best druggability 0.73). MolNFT v1 #149048 on…
- 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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