Research workbench
Crystal structure of copk bound to CU(I) and CU(II)
Analyse Crystal structure of copk bound to CU(I) and CU(II) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3N7D
- Type
- protein
- Length
- 114 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper resistance protein K
- UniProt
- Q58AD3
- Ligands
- CU, CU1
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper resistance protein K | protein | 59 | 0% helix, 53% strand | Q58AD3 |
| B | Copper resistance protein K | protein | 55 | 0% helix, 51% strand | Q58AD3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 660 Ų buried · 14 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 Q58AD3
- Elsewhere: RCSB PDB 3N7D · PDBe 3N7D · UniProt Q58AD3
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