MolNFT v1 · #50755 · protein
COPPER(I) loaded form of the first domain of the human copper chaperone for SOD1, ccs
2RSQ · Copper chaperone for superoxide dismutase: “COPPER(I) loaded form of the first domain of the human copper chaperone for SOD1, ccs”. Solution nmr, 1 ligand (CU1). MolNFT v1 #50755 on GenesisL1: 3D structure, binding sites and pockets…
- 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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