Research workbench
Crystal structure of fosfomycin resistance kinase foma from streptomyces wedmorensis complexed with mgadp and fosfomycin vanadate
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
- 3QVF
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Foma protein
- UniProt
- Q56187
- Ligands
- ADP, FV1, MG
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Foma protein | protein | 274 | 36% helix, 22% strand | Q56187 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- FV1 · dihydroxy{[(2R,3S)-3-methyloxiran-2-yl]phosphonato-kappaO}oxovanadium · 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
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 | 222 | 0.66 | 0.84 | 40 | ADP, FV1, MG |
| 2 | 61 | 0.47 | 0.84 | 16 | empty |
| 3 | 58 | 0.37 | 0.79 | 14 | empty |
Compared structures
- 3QVF · 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 3QVF · PDBe 3QVF · UniProt Q56187
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