Download MendeleyCrystal structure of Type III pantothenate kinase from Burkholderia thailandensis, apo structure
Seattle Structural Genomics Center for Infectious Disease, Abendroth, J., Lorimer, D., Edwards, T.E.To be published.
4O8K
Crystal structure of Type III pantothenate kinase from Burkholderia thailandensis, apo structure
- PDB DOI: https://doi.org/10.2210/pdb4O8K/pdb
- Classification: TRANSFERASE
- Organism(s): Burkholderia thailandensis E264
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2013-12-28 Released: 2014-01-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.186
- R-Value Work: 0.162
- R-Value Observed: 0.163
wwPDB Validation 3D Report Full Report
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 |
| Type III pantothenate kinase | 280 | Burkholderia thailandensis E264 | Mutation(s): 0 Gene Names: BTH_I0369, coaX EC: 2.7.1.33 |  | |
UniProt | |||||
Find proteins for Q2T1M2 (Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264)) Explore Q2T1M2 Go to UniProtKB: Q2T1M2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q2T1M2 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PO4 Query on PO4 | F [auth B] | PHOSPHATE ION O4 P NBIIXXVUZAFLBC-UHFFFAOYSA-K |  | ||
| EDO Query on EDO | C [auth A] D [auth A] G [auth B] H [auth B] I [auth B] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| CL Query on CL | E [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.186
- R-Value Work: 0.162
- R-Value Observed: 0.163
- Space Group: P 43 21 2
- Diffraction Data: https://doi.org/10.18430/M34O8K
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 95.94 | α = 90 |
| b = 95.94 | β = 90 |
| c = 109.2 | γ = 90 |
| Software Name | Purpose |
|---|---|
| XSCALE | data scaling |
| PHASER | phasing |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| BOS | data collection |
| XDS | data reduction |
Entry History
Deposition Data
- Released Date: 2014-01-15 Deposition Author(s): Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Revision History (Full details and data files)
- Version 1.0: 2014-01-15
Type: Initial release - Version 1.1: 2018-01-24
Changes: Structure summary - Version 1.2: 2023-09-20
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.3: 2023-12-06
Changes: Data collection
