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Crystal structure of Certhrax catalytic domain
Analyse Crystal structure of Certhrax catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FK7
- Type
- protein
- Length
- 203 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.78
- Source
- Bacillus cereus
- Molecule
- Putative ADP-ribosyltransferase Certhrax
- EC
- 2.4.2.-
- UniProt
- Q4MV79
- Ligands
- P34, UNX, CL
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · resolution 1.78 · 1 distinct chain · 38% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ADP-ribosyltransferase Certhrax (EC 2.4.2.-) | protein | 203 | 38% helix, 27% strand | Q4MV79 |
Ligands and binding sites
- P34 · N~2~,N~2~-dimethyl-N~1~-(6-oxo-5,6-dihydrophenanthridin-2-yl)glycinamide · ligand · chains A
- UNX · Unknown atom or ion · ion · 12 copies · chains A
- CL · Chloride ion · ion · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.60 | 0.79 | 38 | P34, UNX |
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 Q4MV79
- Elsewhere: RCSB PDB 4FK7 · PDBe 4FK7 · UniProt Q4MV79
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