Download MendeleyHaloalkane Dehalogenase Family Member from Bacteroides thetaiotaomicron of Unknown Function
Matthew, M.W., Ramagopal, U.A., Toro, R., Dickey, M., Sauder, J.M., Poulter, C.D., Burley, S.K., Gerlt, J.A., Almo, S.C.To be published.
3QNM
Haloalkane Dehalogenase Family Member from Bacteroides thetaiotaomicron of Unknown Function
- PDB DOI: https://doi.org/10.2210/pdb3QNM/pdb
- Classification: Structural genomics, unknown function
- Organism(s): Bacteroides thetaiotaomicron
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2011-02-08 Released: 2011-03-30
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.201
- R-Value Work: 0.166
- R-Value Observed: 0.168
wwPDB Validation 3D Report Full Report
This is version 1.4 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 |
| Haloacid dehalogenase-like hydrolase | 240 | Bacteroides thetaiotaomicron | Mutation(s): 0 Gene Names: BT_2271 |  | |
UniProt | |||||
Find proteins for Q8A5G8 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)) Explore Q8A5G8 Go to UniProtKB: Q8A5G8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8A5G8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CL Query on CL | C [auth A], D [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| MG Query on MG | B [auth A] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.201
- R-Value Work: 0.166
- R-Value Observed: 0.168
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 42.85 | α = 90 |
| b = 51.19 | β = 90 |
| c = 123.01 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CBASS | data collection |
| PHENIX | model building |
| PHENIX | refinement |
| MOSFLM | data reduction |
| SCALA | data scaling |
| PHENIX | phasing |
Entry History
Deposition Data
- Released Date: 2011-03-30 Deposition Author(s): Matthew, M.W., Ramagopal, U.A., Toro, R., Dickey, M., Sauder, J.M., Poulter, C.D., Burley, S.K., Gerlt, J.A., Almo, S.C., New York SGX Research Center for Structural Genomics (NYSGXRC)
Revision History (Full details and data files)
- Version 1.0: 2011-03-30
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2018-11-21
Changes: Data collection, Structure summary - Version 1.3: 2021-02-10
Changes: Database references, Derived calculations, Structure summary - Version 1.4: 2024-11-27
Changes: Data collection, Database references, Structure summary
