Research workbench
Crystal structure of human copper homeostatic proteins ATOX1
Analyse Crystal structure of human copper homeostatic proteins ATOX1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DC1
- Type
- protein
- Length
- 134 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper transport protein ATOX1
- UniProt
- O00244
- Ligands
- AG
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper transport protein ATOX1 | protein | 68 | 31% helix, 35% strand | O00244 |
| B | Copper transport protein ATOX1 | protein | 66 | 35% helix, 33% strand | O00244 |
Ligands and binding sites
- AG · Silver ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 743 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7DC1 · Crystal structure of human copper homeostatic proteins atox1 · the same entry in another collection · chain A against A, TM-score 1.00
- O00244 · AlphaFold monomer V2.0 prediction for copper transport protein ATOX1 (O00244) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 O00244
- Elsewhere: RCSB PDB 7DC1 · PDBe 7DC1 · UniProt O00244
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