Research workbench
Bacillus cereus coth kinase
Analyse Bacillus cereus coth kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JD9
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spore coat protein H
- UniProt
- Q739M5
- Ligands
- MG
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spore coat protein H | protein | 358 | 39% helix, 23% strand | Q739M5 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.62 | 0.79 | 49 | MG |
| 2 | 80 | 0.47 | 0.82 | 18 | EDO |
| 3 | 76 | 0.42 | 0.80 | 14 | empty |
| 4 | 58 | 0.34 | 0.77 | 14 | empty |
Compared structures
- 5JD9 · Bacillus cereus CotH kinase · 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 Q739M5
- Elsewhere: RCSB PDB 5JD9 · PDBe 5JD9 · UniProt Q739M5
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