Research workbench
Domain II of the human copper chaperone for superoxide dismutase at 1.55 a resolution
Analyse Domain II of the human copper chaperone for superoxide dismutase at 1.55 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FN8
- Type
- protein
- Length
- 303 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper chaperone for superoxide dismutase
- UniProt
- O14618
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper chaperone for superoxide dismutase | protein | 151 | 6% helix, 42% strand | O14618 |
| B | Copper chaperone for superoxide dismutase | protein | 152 | 5% helix, 40% strand | O14618 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 139 | 0.42 | 0.75 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 782 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6FN8 · Domain II of the HUMAN COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE at 1.55 A resolution · 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 0.99
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
- Elsewhere: RCSB PDB 6FN8 · PDBe 6FN8 · UniProt O14618
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