Download MendeleyCrystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (UDP-N-acetylglucosamine enolpyruvyl transferase, EPT) from Pseudomonas aeruginosa
Abendroth, J., Dranow, D.M., Lorimer, D.D., Edwards, T.E.To be published.
5BQ2
Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (UDP-N-acetylglucosamine enolpyruvyl transferase, EPT) from Pseudomonas aeruginosa
- PDB DOI: https://doi.org/10.2210/pdb5BQ2/pdb
- Classification: TRANSFERASE
- Organism(s): Pseudomonas aeruginosa PAO1
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2015-05-28 Released: 2015-07-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.181
- R-Value Work: 0.148
- R-Value Observed: 0.150
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 |
| UDP-N-acetylglucosamine 1-carboxyvinyltransferase | 429 | Pseudomonas aeruginosa PAO1 | Mutation(s): 0 Gene Names: murA, PA4450 EC: 2.5.1.7 |  | |
UniProt | |||||
Find proteins for Q9HVW7 (Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)) Explore Q9HVW7 Go to UniProtKB: Q9HVW7 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9HVW7 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EPU Query on EPU | E [auth A], G [auth B], I [auth C], L [auth D] | URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID C20 H29 N3 O19 P2 BEGZZYPUNCJHKP-DBYWSUQTSA-N |  | ||
| MG Query on MG | F [auth A] H [auth B] J [auth C] K [auth C] M [auth D] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| QPA Query on QPA | A, B, C, D | L-PEPTIDE LINKING | C6 H12 N O8 P S |  | CYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.181
- R-Value Work: 0.148
- R-Value Observed: 0.150
- Space Group: P 21 21 2
- Diffraction Data: https://doi.org/10.18430/M35BQ2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 130.17 | α = 90 |
| b = 166.81 | β = 90 |
| c = 81.45 | γ = 90 |
| Software Name | Purpose |
|---|---|
| XDS | data reduction |
| XSCALE | data scaling |
| PHASER | phasing |
| ARP | model building |
| Coot | model building |
| PHENIX | refinement |
Entry History
Deposition Data
- Released Date: 2015-07-15 Deposition Author(s): SSGCID, Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Revision History (Full details and data files)
- Version 1.0: 2015-07-15
Type: Initial release - Version 1.1: 2023-09-27
Changes: Advisory, Data collection, Database references, Derived calculations, Refinement description, Source and taxonomy - Version 1.2: 2023-11-15
Changes: Data collection
