Research workbench
Crystal structure of the copper chaperone nosl from shewanella denitrificans
Analyse Crystal structure of the copper chaperone nosl from shewanella denitrificans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OG7
- Type
- protein
- Length
- 134 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nosl
- UniProt
- Q12M31
- Ligands
- CCN, CU1, ZN
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nosl | protein | 134 | 19% helix, 31% strand | Q12M31 |
Ligands and binding sites
- CCN · Acetonitrile · ligand · 5 copies · chains A
- CU1 · Copper (I) ion · metal · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7OG7 · Crystal structure of the copper chaperone NosL from Shewanella denitrificans · the same entry in another collection · chain A against A, TM-score 1.00
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 Q12M31
- Elsewhere: RCSB PDB 7OG7 · PDBe 7OG7 · UniProt Q12M31
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.