Download MendeleyCrystal structure of Bacillus subtilis UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP
Yang, C.S., Chen, S.C., Kuan, S.M., Chen, Y.R., Liu, Y.H., Chen, Y.To be published.
4FKZ
Crystal structure of Bacillus subtilis UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP
- PDB DOI: https://doi.org/10.2210/pdb4FKZ/pdb
- Classification: BIOSYNTHETIC PROTEIN
- Organism(s): Bacillus subtilis subsp. subtilis str. 168
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2012-06-14 Released: 2013-05-08
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.69 ?
- R-Value Free: 0.199
- R-Value Work: 0.170
- R-Value Observed: 0.172
Starting Model: experimental
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This is version 1.1 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 |
| UDP-N-acetylglucosamine 2-epimerase | 388 | Bacillus subtilis subsp. subtilis str. 168 | Mutation(s): 0 Gene Names: BSU35660, mnaA EC: 5.1.3.14 |  | |
UniProt | |||||
Find proteins for P39131 (Bacillus subtilis (strain 168)) Explore P39131 Go to UniProtKB: P39131 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P39131 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| UD1 Query on UD1 | C [auth A], E [auth B] | URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE C17 H27 N3 O17 P2 LFTYTUAZOPRMMI-CFRASDGPSA-N |  | ||
| UDP Query on UDP | D [auth A], F [auth B] | URIDINE-5'-DIPHOSPHATE C9 H14 N2 O12 P2 XCCTYIAWTASOJW-XVFCMESISA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.69 ?
- R-Value Free: 0.199
- R-Value Work: 0.170
- R-Value Observed: 0.172
- Space Group: P 21 21 2
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 91.289 | ¦Á = 90 |
| b = 209.338 | ¦Â = 90 |
| c = 46.81 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| PHASER | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2013-05-08 Deposition Author(s): Yang, C.S., Chen, S.C., Kuan, S.M., Chen, Y.R., Liu, Y.H., Chen, Y.
Revision History (Full details and data files)
- Version 1.0: 2013-05-08
Type: Initial release - Version 1.1: 2023-09-13
Changes: Data collection, Database references, Derived calculations, Refinement description
