Download MendeleyBiochemical Investigation of the Enzymes Required for the Production of 2,3,4-triacetoamido-2,3,4-trideoxy-l-arabinose in Psychrobacter cryohalolentis K5
Bockhaus, N.J., Dunsirn, M.M., Thoden, J.B., Holden, H.M.To be published.
8VR3
crystal structure of the Pcryo_0618 aminotransferase from Psychrobacter cryohalolentis K5 in the presence of its internal aldimine
- PDB DOI: https://doi.org/10.2210/pdb8VR3/pdb
- Classification: TRANSFERASE
- Organism(s): Psychrobacter cryohalolentis K5
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2024-01-20 Released: 2024-01-31
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.233
- R-Value Work: 0.198
- R-Value Observed: 0.199
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 |
| DegT/DnrJ/EryC1/StrS aminotransferase | 374 | Psychrobacter cryohalolentis K5 | Mutation(s): 0 Gene Names: Pcryo_0618 |  | |
UniProt | |||||
Find proteins for Q1QD52 (Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5)) Explore Q1QD52 Go to UniProtKB: Q1QD52 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q1QD52 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| A1ADI Query on A1ADI | F [auth B], G [auth B] | 2,2'-(1,4-diazepane-1,4-diyl)di(ethane-1-sulfonic acid) C9 H20 N2 O6 S2 QZTMPPUJIVQNKS-UHFFFAOYSA-N |  | ||
| EDO Query on EDO | C [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| CL Query on CL | H [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| NA Query on NA | D [auth A], E [auth A] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| LLP Query on LLP | A, B | L-PEPTIDE LINKING | C14 H22 N3 O7 P |  | LYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.233
- R-Value Work: 0.198
- R-Value Observed: 0.199
- Space Group: C 2 2 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 116.019 | α = 90 |
| b = 157.97 | β = 90 |
| c = 130.591 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SAINT | data reduction |
| SADABS | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2024-01-31 Deposition Author(s): Bockhaus, N.J., Thoden, J.B., Holden, H.M.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | R35 GM134643 |
Revision History (Full details and data files)
- Version 1.0: 2024-01-31
Type: Initial release
