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Crystal structure of cadmium-HAH1
Analyse Crystal structure of cadmium-HAH1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FE0
- 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
- GLC, FRU, CD, SO4
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper transport protein ATOX1 | protein | 66 | 35% helix, 35% strand | O00244 |
| B | Copper transport protein ATOX1 | protein | 68 | 34% helix, 35% strand | O00244 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains B
- FRU · beta-D-fructofuranose · sugar · chains A, B
- CD · Cadmium ion · metal · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.27 | 0.73 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 528 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
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 1FE0 · PDBe 1FE0 · UniProt O00244
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