Research workbench
GLNK1 from methanocaldococcus jannaschii with mg-ATP and 2- oxoglutarate at a resolution of 1.2 a
Analyse GLNK1 from methanocaldococcus jannaschii with mg-ATP and 2- oxoglutarate at a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P52
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrogen regulatory protein GLNK1
- UniProt
- Q60381
- Ligands
- ATP, AKG, MG, NO3
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrogen regulatory protein GLNK1 | protein | 112 | 29% helix, 38% strand | Q60381 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- AKG · 2-oxoglutaric acid · ligand · chains A
- MG · Magnesium ion · metal · chains A
- NO3 · Nitrate ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.40 | 0.77 | 19 | ATP, AKG, MG |
Modifications
Observed in the structure: 1 modified (formylation).
Compared structures
- 7P52 · GlnK1 from Methanocaldococcus jannaschii with Mg-ATP and 2-oxoglutarate at a resolution… · the same entry in another collection · chain A against A, TM-score 1.00
- Q60381 · AlphaFold monomer V2.0 prediction for uncharacterized nitrogen regulatory pii-like… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q60381
- Elsewhere: RCSB PDB 7P52 · PDBe 7P52 · UniProt Q60381
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