Research workbench
Structural basis for the specialization of nur, a nickel- specific fur homologue, in metal sensing and DNA recognition
Analyse Structural basis for the specialization of nur, a nickel- specific fur… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EYY
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative iron uptake regulatory protein
- UniProt
- Q9K4F8
- Ligands
- NI, ZN, CL
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative iron uptake regulatory protein | protein | 133 | 44% helix, 21% strand | Q9K4F8 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 5 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
- MLI · Malonate ion · additive · 3 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 · 1253 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3EYY · Structural basis for the specialization of Nur, a nickel-specific Fur homologue, in metal… · 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 Q9K4F8
- Elsewhere: RCSB PDB 3EYY · PDBe 3EYY · UniProt Q9K4F8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.