Research workbench
Solution structure and backbone dynamics of the CU(I) form of the second metal-binding domain of the menkes protein ATP7A
Analyse Solution structure and backbone dynamics of the CU(I) form of the second… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S6U
- Type
- protein
- Length
- 76 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper-transporting ATPase 1
- EC
- 3.6.3.4
- UniProt
- Q04656
- Ligands
- CU1
Structure
solution nmr · 1 distinct chain · 32% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper-transporting ATPase 1 (EC 3.6.3.4) | protein | 76 | 32% helix, 32% strand | Q04656 |
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
- 1S6U · Solution structure and backbone dynamics of the Cu(I) form of the second metal-binding… · the same entry in another collection · chain A against A, TM-score 1.00
- Q04656 · AlphaFold monomer V2.0 prediction for copper-transporting ATPase 1 (Q04656) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 Q04656
- Elsewhere: RCSB PDB 1S6U · PDBe 1S6U · UniProt Q04656
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