Research workbench
Crystal structure of fosfomycin resistance kinase foma from streptomyces wedmorensis complexed with mgatp
Analyse Crystal structure of fosfomycin resistance kinase foma from streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QUN
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Foma protein
- UniProt
- Q56187
- Ligands
- ATP, MG
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Foma protein | protein | 247 | 35% helix, 25% strand | Q56187 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.46 | 0.85 | 16 | empty |
| 2 | 87 | 0.32 | 0.74 | 21 | MG, GOL |
Compared structures
- 3QUN · Crystal structure of fosfomycin resistance kinase FomA from Streptomyces wedmorensis… · 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 Q56187
- Elsewhere: RCSB PDB 3QUN · PDBe 3QUN · UniProt Q56187
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