Download MendeleyHuman FDPS Synthase in Complex with a Rigid Analog of Risedronate
Evdokimov, A.G., Barnett, B.L., Ebetino, F.H., Pokross, M.To be published.
3S4J | pdb_00003s4j
Human FDPS Synthase in Complex with a Rigid Analog of Risedronate
- PDB DOI: https://doi.org/10.2210/pdb3S4J/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2011-05-19 Released: 2011-06-29
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.231 (Depositor), 0.230 (DCC)
- R-Value Work: 0.188 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.188 (Depositor)
Starting Model: experimental
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This is version 1.2 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 synthase | 349 | Homo sapiens | Mutation(s): 1 Gene Names: FDPS, FPS, KIAA1293 EC: 2.5.1.10 (PDB Primary Data), 2.5.1.1 (PDB Primary Data) |  | |
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 | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| UNV Query on UNV | B [auth A] | 6,7-dihydro-5H-cyclopenta[b]pyridine-6,6-diylbis(phosphonic acid) C8 H11 N O6 P2 BKUBDCZNHKIXPI-UHFFFAOYSA-N |  | ||
| SO4 Query on SO4 | F [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| MG Query on MG | 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: 0.231 (Depositor), 0.230 (DCC)
- R-Value Work: 0.188 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.188 (Depositor)
Space Group: P 41 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 111.198 | α = 90 |
| b = 111.198 | β = 90 |
| c = 69.598 | γ = 90 |
| Software Name | Purpose |
|---|---|
| MAR345dtb | data collection |
| AMoRE | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| SCALEPACK | data scaling |
Entry History
Deposition Data
- Released Date: 2011-06-29 Deposition Author(s): Evdokimov, A.G., Barnett, B.L., Ebetino, F.H., Pokross, M.
Revision History (Full details and data files)
- Version 1.0: 2011-06-29
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2023-09-13
Changes: Data collection, Database references, Derived calculations, Refinement description
