MolNFT v1 · #104907 · protein
Crystal structure of human copper chaperone bound to the platinum ion
4QOT · Copper transport protein ATOX1: “Crystal structure of human copper chaperone bound to the platinum ion”. X-ray diffraction, 2 ligands (PT, SO4). MolNFT v1 #104907 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4QOT
- Type
- protein
- Length
- 134 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper transport protein ATOX1
- EC
- 3.6.3.54
- UniProt
- O00244
- Ligands
- PT, SO4
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Copper transport protein ATOX1 (EC 3.6.3.54) | protein | 67 | 34% helix, 34% strand | O00244 |
Ligands and binding sites
- PT · Platinum (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 5 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 · 513 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4QOT · Crystal structure of human copper chaperone bound to the platinum ion · the same entry in another collection · chain B against B, 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 0.99
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 4QOT · PDBe 4QOT · UniProt O00244
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