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Crystal structure of L. major mevalonate kinase
Analyse Crystal structure of L. major mevalonate kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HFS
- Type
- protein
- Length
- 652 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mevalonate kinase, putative
- EC
- 2.7.1.36
- UniProt
- Q4Q6K7
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Mevalonate kinase, putative (EC 2.7.1.36) | protein | 326 | 44% helix, 24% strand | Q4Q6K7 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 463 | 0.75 | 0.84 | 56 | empty |
| 2 | 479 | 0.71 | 0.81 | 54 | empty |
| 3 | 105 | 0.63 | 0.89 | 21 | empty |
| 4 | 91 | 0.39 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1057 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2HFS · Crystal structure of L. major mevalonate 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 Q4Q6K7
- Elsewhere: RCSB PDB 2HFS · PDBe 2HFS · UniProt Q4Q6K7
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