Download MendeleyX-ray crystal structure of PAS domain of HTR-like protein from Haloarcula marismortui.
Osipiuk, J., Zhou, M., Freeman, L., Joachimiak, A.To be published.
3BWL
Crystal structure of PAS domain of HTR-like protein from Haloarcula marismortui
- PDB DOI: https://doi.org/10.2210/pdb3BWL/pdb
- Classification: TRANSFERASE
- Organism(s): Haloarcula marismortui ATCC 43049
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2008-01-09 Released: 2008-01-15
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.73 Å
- R-Value Free: 0.197
- R-Value Work: 0.159
- R-Value Observed: 0.161
wwPDB Validation 3D Report Full Report
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 |
| Sensor protein | 126 | Haloarcula marismortui ATCC 43049 | Mutation(s): 0 Gene Names: htlD, rrnAC0075 EC: 2.7.13.3 |  | |
UniProt | |||||
Find proteins for Q5V5P7 (Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)) Explore Q5V5P7 Go to UniProtKB: Q5V5P7 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5V5P7 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| I3A Query on I3A | F [auth A], H [auth B], J [auth C], M [auth D] | 1H-INDOLE-3-CARBALDEHYDE C9 H7 N O OLNJUISKUQQNIM-UHFFFAOYSA-N |  | ||
| MG Query on MG | E [auth A], G [auth B], I [auth C], K [auth D], L [auth D] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C, D | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.73 Å
- R-Value Free: 0.197
- R-Value Work: 0.159
- R-Value Observed: 0.161
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 66.811 | α = 90 |
| b = 68.533 | β = 90 |
| c = 105.988 | γ = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | phasing |
| SOLVE | phasing |
| RESOLVE | phasing |
| HKL-3000 | phasing |
Entry History
Deposition Data
- Released Date: 2008-01-15 Deposition Author(s): Osipiuk, J., Zhou, M., Freeman, L., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-01-15
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2024-11-20
Changes: Data collection, Database references, Derived calculations, Structure summary
