Research workbench
COPPER(I) loaded form of the first domain of the human copper chaperone for SOD1, ccs
Analyse COPPER(I) loaded form of the first domain of the human copper chaperone for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RSQ
- Type
- protein
- Length
- 71 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper chaperone for superoxide dismutase
- UniProt
- O14618
- Ligands
- CU1
Structure
solution nmr · 1 distinct chain · 28% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper chaperone for superoxide dismutase | protein | 71 | 28% helix, 37% strand | O14618 |
Ligands and binding sites
- CU1 · Copper (I) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2RSQ · Copper(I) loaded form of the first domain of the human copper chaperone for SOD1, CCS · 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 0.94
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 2RSQ · PDBe 2RSQ · UniProt O14618
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