Download MendeleyCrystal Structure of Uncharacterized protein Aaci_0196 from Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446
Wu, R., Bedearn, J., Joachimiak, A.To be published.
3RAG
Crystal Structure of Uncharacterized protein Aaci_0196 from Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446
- PDB DOI: https://doi.org/10.2210/pdb3RAG/pdb
- Classification: Structural Genomics, Unknown function
- Organism(s): Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2011-03-28 Released: 2011-09-14
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.215
- R-Value Work: 0.193
- R-Value Observed: 0.194
wwPDB Validation 3D Report Full Report
This is version 1.1 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 |
| uncharacterized protein | 242 | Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446 | Mutation(s): 0 Gene Names: Aaci_0196 |  | |
UniProt | |||||
Find proteins for C8WQT1 (Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA)) Explore C8WQT1 Go to UniProtKB: C8WQT1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | C8WQT1 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | D [auth A], E [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| NA Query on NA | C [auth A], F [auth B] | SODIUM ION Na FKNQFGJONOIPTF-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: 1.80 Å
- R-Value Free: 0.215
- R-Value Work: 0.193
- R-Value Observed: 0.194
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 46.696 | α = 90 |
| b = 85.889 | β = 90 |
| c = 132.971 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-3000 | data collection |
| MLPHARE | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
Entry History
Deposition Data
- Released Date: 2011-09-14 Deposition Author(s): Wu, R., Bedearn, J., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2011-09-14
Type: Initial release - Version 1.1: 2011-12-14
Changes: Structure summary
