Download MendeleyHuman farnesyl diphosphate synthase complexed with MG and minodronate.
Pilka, E.S., Dunford, J.E., Guo, K., Pike, A.C.W., Kavanagh, K.L., von Delft, F., Ebetino, F.H., Arrowsmith, C.H., Edwards, A.M., Russell, R.G.G., Oppermann, U.To be published.
3B7L
Human farnesyl diphosphate synthase complexed with MG and minodronate
- PDB DOI: https://doi.org/10.2210/pdb3B7L/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2007-10-31 Released: 2007-11-13
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.202
- R-Value Work: 0.169
- R-Value Observed: 0.171
Starting Model: experimental
View more details
This is version 1.3 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Farnesyl pyrophosphate synthetase | 356 | Homo sapiens | Mutation(s): 0 Gene Names: FDPS, FPS, KIAA1293 EC: 2.5.1.10 (PDB Primary Data), 2.5.1.1 (UniProt) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P14324 (Homo sapiens) Explore P14324 Go to UniProtKB: P14324 | |||||
PHAROS: P14324 GTEx: ENSG00000160752 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P14324 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| M0N Query on M0N | F [auth A] | (1-HYDROXY-2-IMIDAZO[1,2-A]PYRIDIN-3-YLETHANE-1,1-DIYL)BIS(PHOSPHONIC ACID) C9 H12 N2 O7 P2 VMMKGHQPQIEGSQ-UHFFFAOYSA-N |  | ||
| MG Query on MG | B [auth A], C [auth A], D [auth A], E [auth A] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.202
- R-Value Work: 0.169
- R-Value Observed: 0.171
- Space Group: P 41 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 110.922 | α = 90 |
| b = 110.922 | β = 90 |
| c = 67.308 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| CrystalClear | data collection |
| MOSFLM | data reduction |
| SCALA | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2007-11-13 Deposition Author(s): Pilka, E.S., Dunford, J.E., Guo, K., Pike, A.C.W., Kavanagh, K.L., von Delft, F., Ebetino, F.H., Arrowsmith, C.H., Edwards, A.M., Russell, R.G.G., Oppermann, U., Structural Genomics Consortium (SGC)
Revision History (Full details and data files)
- Version 1.0: 2007-11-13
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2018-01-31
Changes: Database references, Structure summary - Version 1.3: 2023-08-30
Changes: Data collection, Database references, Derived calculations, Refinement description
