Download MendeleyConformational transitions, ligand specificity and catalysis in N-acetylornithine aminotransferase: Implications on drug designing and rational enzyme engineering in omega aminotransferases.
Bisht, S., Bharath, S.R., Murthy, M.R.N.To be published.
4JEV
N-acetylornithine aminotransferase from S. typhimurium complexed with gabaculine
- PDB DOI: https://doi.org/10.2210/pdb4JEV/pdb
- Classification: TRANSFERASE
- Organism(s): Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2013-02-27 Released: 2014-03-26
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.67 Å
- R-Value Free: 0.188
- R-Value Work: 0.163
- R-Value Observed: 0.164
Starting Model: experimental
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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 |
| Acetylornithine/succinyldiaminopimelate aminotransferase | 422 | Salmonella enterica subsp. enterica serovar Typhimurium str. LT2 | Mutation(s): 1 Gene Names: argD, dapC, dtu, STM3468 EC: 2.6.1.11 (PDB Primary Data), 2.6.1.17 (PDB Primary Data) |  | |
UniProt | |||||
Find proteins for P40732 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)) Explore P40732 Go to UniProtKB: P40732 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P40732 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PXG Query on PXG | C [auth A], F [auth B] | 3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC ACID C15 H17 N2 O7 P WSOQXCGRIUHULI-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | D [auth A], G [auth B] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| NA Query on NA | E [auth A], H [auth B] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| CSO Query on CSO | A, B | L-PEPTIDE LINKING | C3 H7 N O3 S |  | CYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.67 Å
- R-Value Free: 0.188
- R-Value Work: 0.163
- R-Value Observed: 0.164
- Space Group: P 21 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 96.66 | α = 90 |
| b = 111.86 | β = 90 |
| c = 65.17 | γ = 90 |
| Software Name | Purpose |
|---|---|
| MAR345dtb | data collection |
| PHASER | phasing |
| REFMAC | refinement |
| MOSFLM | data reduction |
| SCALA | data scaling |
Entry History
Deposition Data
- Released Date: 2014-03-26 Deposition Author(s): Bisht, S., Bharath, S.R., Murthy, M.R.N.
Revision History (Full details and data files)
- Version 1.0: 2014-03-26
Type: Initial release - Version 1.1: 2023-11-08
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.2: 2023-12-06
Changes: Data collection - Version 1.3: 2024-10-09
Changes: Structure summary
