Research workbench
Crystal structure of fpps in complex with zoledronate
Analyse Crystal structure of fpps in complex with zoledronate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F8C
- Type
- protein
- Length
- 343 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Farnesyl diphosphate synthase
- EC
- 2.5.1.1, 2.5.1.10
- UniProt
- P14324
- Ligands
- ZOL, MG, PO4
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | Farnesyl diphosphate synthase (EC 2.5.1.1, 2.5.1.10) | protein | 343 | 74% helix, 1% strand | P14324 |
Ligands and binding sites
- ZOL · Zoledronic acid · ligand · chains F
- MG · Magnesium ion · metal · 3 copies · chains F
- PO4 · Phosphate ion · ion · chains F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.77 | 0.87 | 53 | PO4, MG, ZOL |
Compared structures
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 P14324
- Elsewhere: RCSB PDB 2F8C · PDBe 2F8C · UniProt P14324
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