MolNFT v1 · #97782 · protein
Crystal structure of human farnesyl pyrophosphate synthase (Y204F) mutant complexed with mg, risedronate and isopentenyl pyrophosphate
4KPD: “Crystal structure of human farnesyl pyrophosphate synthase (Y204F) mutant complexed with mg, risedronate and…”. X-ray diffraction, 3 ligands (IPE, RIS, MG), 1 pocket (best druggability 0.82). MolNFT v1 #97782 on GenesisL1: 3D…
- PDB
- 4KPD
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Farnesyl pyrophosphate synthase
- EC
- 2.5.1.10, 2.5.1.1
- UniProt
- P14324
- Ligands
- IPE, RIS, MG
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Farnesyl pyrophosphate synthase (EC 2.5.1.10, 2.5.1.1) | protein | 341 | 74% helix, 1% strand | P14324 |
Ligands and binding sites
- IPE · 3-methylbut-3-enyl trihydrogen diphosphate · ligand · chains A
- RIS · 1-hydroxy-2-(3-pyridinyl)ethylidene bis-phosphonic acid · ligand · chains A
- MG · Magnesium ion · metal · 3 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 | 283 | 0.82 | 0.93 | 47 | MG, IPE, RIS |
Compared structures
- 4KPD · Crystal Structure of Human Farnesyl Pyrophosphate Synthase (Y204F) Mutant Complexed with… · 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 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 P14324
- Elsewhere: RCSB PDB 4KPD · PDBe 4KPD · UniProt P14324
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