Research workbench
Human farnesyl diphosphate synthase complexed with bisphosphonate bph- 527
Analyse Human farnesyl diphosphate synthase complexed with bisphosphonate bph- 527 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OPN
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Farnesyl pyrophosphate synthetase (fpp synthetase) (fps) (farnesyl diphosphate…
- EC
- 2.5.1.10
- UniProt
- P14324
- Ligands
- SUF, MG, PO4
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Farnesyl pyrophosphate synthetase (fpp synthetase) (fps) (farnesyl diphosphate synthetase) [includes: dimethylallyltranstransferase (ec 2.5.1.1) (EC 2.5.1.10) | protein | 336 | 73% helix, 1% strand | P14324 |
Ligands and binding sites
- SUF · [2-(dimethyl-lambda~4~-sulfanyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid) · ligand · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
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 | 551 | 0.77 | 0.84 | 60 | MG, PO4, SUF |
Compared structures
- 2OPN · Human Farnesyl Diphosphate Synthase Complexed with Bisphosphonate BPH-527 · the same entry in another collection · chain A against A, TM-score 1.00
- P14324 · AlphaFold monomer V2.0 prediction for farnesyl pyrophosphate synthase (P14324) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 2OPN · PDBe 2OPN · UniProt P14324
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