Research workbench
Glnk, a signal protein from E. COLI
Analyse Glnk, a signal protein from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GNK
- Type
- protein
- Length
- 95 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Escherichia coli
- Molecule
- Protein (nitrogen regulatory protein)
- UniProt
- P0AC55
- Ligands
- ATP
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 34% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (nitrogen regulatory protein) | protein | 95 | 34% helix, 34% strand | P0AC55 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P0AC55
- Elsewhere: RCSB PDB 2GNK · PDBe 2GNK · UniProt P0AC55
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