Download MendeleyImpact of the Carboxylated Lysine on the Acylation and Deacylation Step in Class D Beta-Lactamase
Vercheval, L., Kerff, F., Bauvois, C., Sauvage, E., Guiet, R., Borel, F., Ferrer, J.L., Charlier, P., Galleni, M.To be published.
2X02 | pdb_00002x02
CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10 AT 1.35 A RESOLUTION
- PDB DOI: https://doi.org/10.2210/pdb2X02/pdb
- Classification: HYDROLASE
- Organism(s): Pseudomonas aeruginosa
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2009-12-04 Released: 2010-12-08
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.35 Å
- R-Value Free: 0.187 (Depositor), 0.180 (DCC)
- R-Value Work: 0.162 (Depositor), 0.160 (DCC)
- R-Value Observed: 0.163 (Depositor)
Starting Model: experimental
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wwPDB Validation 3D Report Full Report
This is version 1.3 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-10 | 248 | Pseudomonas aeruginosa | Mutation(s): 0 EC: 3.5.2.6 |  | |
UniProt | |||||
Find proteins for P14489 (Pseudomonas aeruginosa) Explore P14489 Go to UniProtKB: P14489 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P14489 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PG4 Query on PG4 | D [auth A], H [auth B] | TETRAETHYLENE GLYCOL C8 H18 O5 UWHCKJMYHZGTIT-UHFFFAOYSA-N |  | ||
| SO4 Query on SO4 | C [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | J [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| DMS Query on DMS | E [auth A], F [auth A], G [auth A], I [auth B] | DIMETHYL SULFOXIDE C2 H6 O S IAZDPXIOMUYVGZ-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| KCX Query on KCX | A, B | L-PEPTIDE LINKING | C7 H14 N2 O4 |  | LYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.35 Å
- R-Value Free: 0.187 (Depositor), 0.180 (DCC)
- R-Value Work: 0.162 (Depositor), 0.160 (DCC)
- R-Value Observed: 0.163 (Depositor)
Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 48.55 | α = 90 |
| b = 96.85 | β = 90 |
| c = 125.74 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| SCALA | data scaling |
| AMoRE | phasing |
Entry History
Deposition Data
- Released Date: 2010-12-08 Deposition Author(s): Vercheval, L., Kerff, F., Sauvage, E., Herman, R., Galleni, M., Charlier, P.
Revision History (Full details and data files)
- Version 1.0: 2010-12-08
Type: Initial release - Version 1.1: 2011-05-08
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2023-12-20
Changes: Data collection, Database references, Derived calculations, Other, Refinement description
