Research workbench
Human copper chaperone for superoxide dismutase domain II
Analyse Human copper chaperone for superoxide dismutase domain II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DO5
- Type
- protein
- Length
- 603 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O14618
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 154 | — | O14618 |
| B, C | — | protein | 148 | — | O14618 |
| D | — | protein | 153 | — | O14618 |
Compared structures
- 1DO5 · Human copper chaperone for superoxide dismutase domain II · the same entry in another collection · chain D against D, 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 C 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 1DO5 · PDBe 1DO5 · UniProt O14618
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