Download MendeleyCrystal structure of hypothetical protein Atu1826, a putative alpha/beta hydrolase from Agrobacterium tumefaciens.
Osipiuk, J., Xu, X., Zheng, H., Savchenko, A., Edwards, A., Joachimiak, A.To be published.
2I3D
Crystal Structure of Protein of Unknown Function ATU1826, a Putative Alpha/Beta Hydrolase from Agrobacterium tumefaciens
- PDB DOI: https://doi.org/10.2210/pdb2I3D/pdb
- Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
- Organism(s): Agrobacterium fabrum str. C58
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2006-08-17 Released: 2006-09-19
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.174
- R-Value Work: 0.138
- R-Value Observed: 0.140
wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| Hypothetical protein Atu1826 | 249 | Agrobacterium fabrum str. C58 | Mutation(s): 6 Gene Names: Atu1826 |  | |
UniProt | |||||
Find proteins for A9CIK7 (Agrobacterium fabrum (strain C58 / ATCC 33970)) Explore A9CIK7 Go to UniProtKB: A9CIK7 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A9CIK7 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CL Query on CL | D [auth A], E [auth A], F [auth A], H [auth B], I [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| MG Query on MG | C [auth A], G [auth B] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.174
- R-Value Work: 0.138
- R-Value Observed: 0.140
- Space Group: P 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 46.549 | α = 92.25 |
| b = 50.579 | β = 115.17 |
| c = 54.844 | γ = 99.82 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SBC-Collect | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| HKL-3000 | phasing |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | phasing |
| SOLVE | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2006-09-19 Deposition Author(s): Osipiuk, J., Xu, X., Zheng, H., Savchenko, A., Edwards, A., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2006-09-19
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Source and taxonomy, Version format compliance
