Research workbench
Crystal structure of NtrC-like two-domain protein (RER070207001320) from Eubacterium rectale at 2.10 A resolution
Analyse Crystal structure of NtrC-like two-domain protein (RER070207001320) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FKQ
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Eubacterium rectale
- Molecule
- NtrC-like two-domain protein
- Ligands
- ATP, MG, CL, SO4
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NtrC-like two-domain protein | protein | 354 | 40% helix, 19% strand | — |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- SO4 · Sulfate ion · ion · chains A
- 2PE · Nonaethylene glycol · additive · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.55 | 0.80 | 29 | empty |
| 2 | 96 | 0.37 | 0.75 | 26 | ATP, MG |
| 3 | 62 | 0.32 | 0.75 | 12 | empty |
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 3FKQ · Crystal structure of ntrc-like two-domain protein (RER070207001320) from eubacterium… · 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
- Elsewhere: RCSB PDB 3FKQ · PDBe 3FKQ
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