Research workbench
The structure of Cu(II)-CopC from Thioalkalivibrio paradoxus
Analyse The structure of Cu(II)-CopC from Thioalkalivibrio paradoxus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8YTR
- Type
- protein
- Length
- 253 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Thioalkalivibrio paradoxus ARh 1
- Molecule
- CopC domain-containing protein
- UniProt
- W0DSL1
- Ligands
- CU
Structure
x-ray diffraction · resolution 1.8 · 2 distinct chains · 10% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CopC domain-containing protein | protein | 127 | 9% helix, 46% strand | W0DSL1 |
| B | CopC domain-containing protein | protein | 126 | 11% helix, 46% strand | W0DSL1 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 828 Ų buried · 14 hydrogen bonds · protein-protein
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 W0DSL1
- Elsewhere: RCSB PDB 8YTR · PDBe 8YTR · UniProt W0DSL1
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