Download MendeleyThe epoxyqueuosine reductase QueH in the biosynthesis of tRNA queuosine is a unique metalloenzyme
Li, Q., Bruner, S.D.To be published.
7LC7
Crystal structure of epoxyqueuosine reductase QueH in complex with GMP from Thermotoga maritima
- PDB DOI: https://doi.org/10.2210/pdb7LC7/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Thermotoga maritima MSB8
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2021-01-09 Released: 2022-01-12
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.58 Å
- R-Value Free: 0.243 (Depositor), 0.240 (DCC)
- R-Value Work: 0.200 (Depositor), 0.200 (DCC)
- R-Value Observed: 0.202 (Depositor)
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 |
| Epoxyqueuosine reductase QueH | 192 | Thermotoga maritima MSB8 | Mutation(s): 0 Gene Names: queH, TM_0731 EC: 1.17.99.6 |  | |
UniProt | |||||
Find proteins for Q9WZJ0 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)) Explore Q9WZJ0 Go to UniProtKB: Q9WZJ0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9WZJ0 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 5GP (Subject of Investigation/LOI) Query on 5GP | C [auth A] | GUANOSINE-5'-MONOPHOSPHATE C10 H14 N5 O8 P RQFCJASXJCIDSX-UUOKFMHZSA-N |  | ||
| SF4 (Subject of Investigation/LOI) Query on SF4 | B [auth A] | IRON/SULFUR CLUSTER Fe4 S4 LJBDFODJNLIPKO-UHFFFAOYSA-N |  | ||
| FE (Subject of Investigation/LOI) Query on FE | D [auth A] | FE (III) ION Fe VTLYFUHAOXGGBS-UHFFFAOYSA-N |  | ||
| CL (Subject of Investigation/LOI) Query on CL | E [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.58 Å
- R-Value Free: 0.243 (Depositor), 0.240 (DCC)
- R-Value Work: 0.200 (Depositor), 0.200 (DCC)
- R-Value Observed: 0.202 (Depositor)
Space Group: C 2 2 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 53.335 | α = 90 |
| b = 104.783 | β = 90 |
| c = 73.741 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XDS | data reduction |
| Aimless | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2022-01-12 Deposition Author(s): Li, Q., Bruner, S.D.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | R01 GM70641 |
Revision History (Full details and data files)
- Version 1.0: 2022-01-12
Type: Initial release - Version 1.1: 2023-10-18
Changes: Data collection, Refinement description
