Download MendeleyStructure of H. Pylori Glutamate Racemace with a crystallographic artifact
Propp, J., Spies, M.A.To be published.
8UDI
Crystal structure of Helicobacter pylori glutamate racemase bound to D-glutamate and a crystallographic artifact
- PDB DOI: https://doi.org/10.2210/pdb8UDI/pdb
- Classification: ISOMERASE
- Organism(s): Helicobacter pylori
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2023-09-28 Released: 2024-10-09
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.10 ?
- R-Value Free: 0.231
- R-Value Work: 0.190
- R-Value Observed: 0.192
Starting Model: experimental
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This is version 1.0 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 |
| Glutamate racemase | 254 | Helicobacter pylori | Mutation(s): 0 Gene Names: murI EC: 5.1.1.3 |  | |
UniProt | |||||
Find proteins for A0A1W0VMR6 (Helicobacter pylori) Explore A0A1W0VMR6 Go to UniProtKB: A0A1W0VMR6 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A1W0VMR6 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| WAW (Subject of Investigation/LOI) Query on WAW | D [auth A] | N-{[(3S)-2-(3-fluoropyrazin-2-yl)-1,2,3,4-tetrahydroisoquinolin-3-yl]methyl}-1H-indazole-4-carboxamide C22 H19 F N6 O GTHUQRDNWWDGLW-INIZCTEOSA-N |  | ||
| DGL Query on DGL | C [auth A], F [auth B] | D-GLUTAMIC ACID C5 H9 N O4 WHUUTDBJXJRKMK-GSVOUGTGSA-N |  | ||
| CL Query on CL | E [auth A], G [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.10 ?
- R-Value Free: 0.231
- R-Value Work: 0.190
- R-Value Observed: 0.192
- Space Group: P 21 21 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 62.317 | ¦Á = 90 |
| b = 81.969 | ¦Â = 90 |
| c = 113.937 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| Aimless | data scaling |
| XDS | data reduction |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2024-10-09 Deposition Author(s): Propp, J., Spies, M.A.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | 1R01GM138471-01 |
Revision History (Full details and data files)
- Version 1.0: 2024-10-09
Type: Initial release
