Research workbench
The biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism
Analyse The biochemical and structural basis for feedback inhibition of mevalonate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R42
- Type
- protein
- Length
- 383 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mevalonate kinase
- EC
- 2.7.1.36
- UniProt
- P17256
- Ligands
- FPS, MG
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mevalonate kinase (EC 2.7.1.36) | protein | 383 | 41% helix, 20% strand | P17256 |
Ligands and binding sites
- FPS · S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl] trihydrogen thiodiphosphate · 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 | 470 | 0.66 | 0.78 | 52 | MG, FPS |
| 2 | 80 | 0.38 | 0.77 | 18 | empty |
| 3 | 55 | 0.32 | 0.77 | 14 | empty |
Compared structures
- 2R42 · The Biochemical and Structural Basis for feedback Inhibition of Mevalonate Kinase and… · the same entry in another collection · chain A against A, TM-score 1.00
- P17256 · AlphaFold monomer V2.0 prediction for mevalonate kinase (P17256) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P17256
- Elsewhere: RCSB PDB 2R42 · PDBe 2R42 · UniProt P17256
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