MolNFT v1 · #72374 · protein
Human fpps complex with NOV_823
3N6K · Farnesyl pyrophosphate synthase: “Human fpps complex with NOV_823”. X-ray diffraction, 2 ligands (BFH, PO4), 1 pocket (best druggability 0.78). MolNFT v1 #72374 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3N6K
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Farnesyl pyrophosphate synthase
- EC
- 2.5.1.1, 2.5.1.10
- UniProt
- P14324
- Ligands
- BFH, PO4
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | Farnesyl pyrophosphate synthase (EC 2.5.1.1, 2.5.1.10) | protein | 341 | 75% helix, 1% strand | P14324 |
Ligands and binding sites
- BFH · 1-(carboxymethyl)-1H-benzo[g]indole-2-carboxylic acid · ligand · 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 | 1035 | 0.78 | 0.80 | 78 | BFH, PO4 |
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 3N6K · PDBe 3N6K · UniProt P14324
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