Research workbench
Central domain of fleq H287A mutant in complex with atpgs and mg
Analyse Central domain of fleq H287A mutant in complex with atpgs and mg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JDL
- Type
- protein
- Length
- 252 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrogen assimilation regulatory protein
- UniProt
- Q51460
- Ligands
- AGS, MG
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrogen assimilation regulatory protein | protein | 252 | 46% helix, 15% strand | Q51460 |
Ligands and binding sites
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.60 | 0.79 | 40 | AGS, MG |
| 2 | 63 | 0.34 | 0.77 | 12 | empty |
Compared structures
- 6JDL · Central domain of FleQ H287A mutant in complex with ATPgS and Mg · 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 Q51460
- Elsewhere: RCSB PDB 6JDL · PDBe 6JDL · UniProt Q51460
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