Download MendeleyEnzyme Mediated Aminoglycoside Resistance Without Target Mimicry
Hemmings, M., Zielinski, M., Golkar, T., Blanchet, J., Pistofidis, A., Munro, K., Schmeing, T.M., Bohle, D.S., Berghuis, A.M.To be published.
9MGT | pdb_00009mgt
Structure of N-3 aminoglycoside acetyltransferase XIa (AAC(3)-XIa) in complex with coenzyme A and tobramycin
- PDB DOI: https://doi.org/10.2210/pdb9MGT/pdb
- Classification: TRANSFERASE
- Organism(s): Corynebacterium striatum
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2024-12-11 Released: 2025-09-03
- Funding Organization(s): Canadian Institutes of Health Research (CIHR)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.96 Å
- R-Value Free: 0.188 (Depositor), 0.187 (DCC)
- R-Value Work: 0.143 (Depositor), 0.141 (DCC)
- R-Value Observed: 0.146 (Depositor)
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 |
| Aminoglycoside N-acetyltransferase AAC(3)-XI | 148 | Corynebacterium striatum | Mutation(s): 0 Gene Names: CBE89_03745 |  | |
UniProt | |||||
Find proteins for A0A0K2X0F2 (Corynebacterium striatum) Explore A0A0K2X0F2 Go to UniProtKB: A0A0K2X0F2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A0K2X0F2 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| COA (Subject of Investigation/LOI) Query on COA | C [auth A], D [auth B] | COENZYME A C21 H36 N7 O16 P3 S RGJOEKWQDUBAIZ-IBOSZNHHSA-N |  | ||
| TOY (Subject of Investigation/LOI) Query on TOY | E [auth B] | TOBRAMYCIN C18 H37 N5 O9 NLVFBUXFDBBNBW-PBSUHMDJSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.96 Å
- R-Value Free: 0.188 (Depositor), 0.187 (DCC)
- R-Value Work: 0.143 (Depositor), 0.141 (DCC)
- R-Value Observed: 0.146 (Depositor)
Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 35.179 | α = 90 |
| b = 101.598 | β = 106.11 |
| c = 39.828 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| PROTEUM PLUS | data reduction |
| PROTEUM PLUS | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-09-03 Deposition Author(s): Zielinski, M., Hemmings, M., Golkar, T., Blanchet, J., Berghuis, A.M.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Canadian Institutes of Health Research (CIHR) | Canada | PJT-162365 |
Revision History (Full details and data files)
- Version 1.0: 2025-09-03
Type: Initial release
