Download MendeleyDual Mechanism of the OXA-23 Carbapenemase Inhibition via Catalytic Lysine Decarboxylation and Water Access Restriction by the Carbapenem NA-1-157
Toth, M., Stewart, N.K., Buynak, J.D., Smith, C.A., Vakulenko, S.B.To be published.
9NT0 | pdb_00009nt0
OXA-23-meropenem, pH 7.5
- PDB DOI: https://doi.org/10.2210/pdb9NT0/pdb
- Classification: HYDROLASE
- Organism(s): Acinetobacter baumannii
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2025-03-17 Released: 2025-08-06
- Funding Organization(s): National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.60 Å
- R-Value Free: 0.202 (Depositor), 0.204 (DCC)
- R-Value Work: 0.167 (Depositor), 0.167 (DCC)
- R-Value Observed: 0.169 (Depositor)
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 |
| Beta-lactamase OXA-23 | 273 | Acinetobacter baumannii | Mutation(s): 0 Gene Names: OXA-23, ari-1, bla-OXA-23, bla_2, bla_3, blaOXA, blaOXA-23, ABUW_0563 EC: 3.5.2.6 |  | |
UniProt | |||||
Find proteins for Q9L4P2 (Acinetobacter baumannii) Explore Q9L4P2 Go to UniProtKB: Q9L4P2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9L4P2 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| MER (Subject of Investigation/LOI) Query on MER | B [auth A] | (4R,5S)-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-5-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-4-methyl-4,5-d
ihydro-1H-pyrrole-2-carboxylic acid C17 H27 N3 O5 S DYQHXZPAIVAJRU-HTXLXMOSSA-N |  | ||
| SO4 Query on SO4 | C [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| KCX Query on KCX | A | L-PEPTIDE LINKING | C7 H14 N2 O4 |  | LYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.60 Å
- R-Value Free: 0.202 (Depositor), 0.204 (DCC)
- R-Value Work: 0.167 (Depositor), 0.167 (DCC)
- R-Value Observed: 0.169 (Depositor)
Space Group: P 42 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 82.991 | α = 90 |
| b = 82.991 | β = 90 |
| c = 85.128 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XDS | data reduction |
| Aimless | data scaling |
| REFMAC | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-08-06 Deposition Author(s): Smith, C.A., Toth, M., Stewart, N.K., Vakulenko, S.B.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) | United States | 1R01 AI155723 |
Revision History (Full details and data files)
- Version 1.0: 2025-08-06
Type: Initial release
