Download MendeleyCrystal structure of IcIR transcriptional regulator from Alicyclobacillus acidocaldarius
Michalska, K., Mack, J.C., Clancy, S., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)To be published.
5TJJ
Crystal structure of IcIR transcriptional regulator from Alicyclobacillus acidocaldarius
- PDB DOI: https://doi.org/10.2210/pdb5TJJ/pdb
- Classification: TRANSCRIPTION
- Organism(s): Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2016-10-04 Released: 2016-10-26
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.234
- R-Value Work: 0.190
- R-Value Observed: 0.192
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 |
| Transcriptional regulator, IclR family | 260 | Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446 | Mutation(s): 0 Gene Names: Aaci_0162 |  | |
UniProt | |||||
Find proteins for C8WQP8 (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 C8WQP8 Go to UniProtKB: C8WQP8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | C8WQP8 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | C [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-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: 2.50 Å
- R-Value Free: 0.234
- R-Value Work: 0.190
- R-Value Observed: 0.192
- Space Group: P 41 21 2
- Diffraction Data: https://doi.org/10.18430/m35tjj
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 98.38 | α = 90 |
| b = 98.38 | β = 90 |
| c = 119.485 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| PHENIX | phasing |
| BUCCANEER | model building |
Entry History & Funding Information
Deposition Data
- Released Date: 2016-10-26 Deposition Author(s): Michalska, K., Mack, J.C., Clancy, S., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | GM094585 |
Revision History (Full details and data files)
- Version 1.0: 2016-10-26
Type: Initial release - Version 1.1: 2017-09-06
Changes: Author supporting evidence, Derived calculations - Version 1.2: 2019-12-25
Changes: Author supporting evidence
