Research workbench
The apo form of hma domain of copper chaperone for superoxide dismutase
Analyse The apo form of hma domain of copper chaperone for superoxide dismutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CRL
- Type
- protein
- Length
- 98 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper chaperone for superoxide dismutase
- UniProt
- O14618
Structure
solution nmr · 1 distinct chain · 18% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper chaperone for superoxide dismutase | protein | 98 | 18% helix, 23% strand | O14618 |
Compared structures
- 2CRL · The apo form of HMA domain of copper chaperone for superoxide dismutase · 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 0.72
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 2CRL · PDBe 2CRL · UniProt O14618
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