Download Mendeley5-Azacytosines as a Novel Scaffold to Inhibit Z. mobilis TGT with Expected Improved Bioavailability and Synthetic Accessibility
Neeb, M., Hohn, C., Heine, A., Diederich, F., Klebe, G.To be published.
4Q4M
tRNA-Guanine Transglycosylase (TGT) in Complex with 6-Amino-4-phenyl-1,2-dihydro-1,3,5-triazin-2-one
- PDB DOI: https://doi.org/10.2210/pdb4Q4M/pdb
- Classification: Transferase/transferase inhibitor
- Organism(s): Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2014-04-15 Released: 2015-06-10
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.62 Å
- R-Value Free: 0.188
- R-Value Work: 0.157
- R-Value Observed: 0.159
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 |
| Queuine tRNA-ribosyltransferase | 386 | Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821 | Mutation(s): 0 Gene Names: tgt, ZMO0363 EC: 2.4.2.29 |  | |
UniProt | |||||
Find proteins for P28720 (Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)) Explore P28720 Go to UniProtKB: P28720 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P28720 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 2YL Query on 2YL | C [auth A] | 6-amino-4-phenyl-1,3,5-triazin-2(1H)-one C9 H8 N4 O ZBKCUYOBOGCDKC-UHFFFAOYSA-N |  | ||
| DMS Query on DMS | D [auth A], E [auth A], F [auth A], G [auth A] | DIMETHYL SULFOXIDE C2 H6 O S IAZDPXIOMUYVGZ-UHFFFAOYSA-N |  | ||
| ZN Query on ZN | B [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.62 Å
- R-Value Free: 0.188
- R-Value Work: 0.157
- R-Value Observed: 0.159
- Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 88.511 | α = 90 |
| b = 63.887 | β = 92.99 |
| c = 70.399 | γ = 90 |
| Software Name | Purpose |
|---|---|
| MAR345dtb | data collection |
| PHASER | phasing |
| PHENIX | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Revision History (Full details and data files)
- Version 1.0: 2015-06-10
Type: Initial release - Version 1.1: 2023-09-20
Changes: Data collection, Database references, Derived calculations, Refinement description
