Download MendeleyCrystal Structure of the Q9WYS3 protein from Thermotoga maritima.
Vorobiev, S., Lew, S., Seetharaman, J., Chi, Y., Xiao, R., Maglaqui, M., Lee, D., Everett, J.K., Acton, T.B., Montelione, G.T., Tong, L., Hunt, J.F.To be published.
4NAR
Crystal Structure of the Q9WYS3 protein from Thermotoga maritima. Northeast Structural Genomics Consortium Target VR152
- PDB DOI: https://doi.org/10.2210/pdb4NAR/pdb
- Classification: ISOMERASE
- Organism(s): Thermotoga maritima MSB8
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2013-10-22 Released: 2013-11-06
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.39 Å
- R-Value Free: 0.229
- R-Value Work: 0.165
- R-Value Observed: 0.168
wwPDB Validation 3D Report Full Report
This is version 1.0 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 |
| Putative uronate isomerase | 435 | Thermotoga maritima MSB8 | Mutation(s): 0 Gene Names: Tmari_0439, TM_0442 |  | |
UniProt | |||||
Find proteins for Q9WYS3 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)) Explore Q9WYS3 Go to UniProtKB: Q9WYS3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9WYS3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | B [auth A], C [auth A], D [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| ACT Query on ACT | E [auth A] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| 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: 2.39 Å
- R-Value Free: 0.229
- R-Value Work: 0.165
- R-Value Observed: 0.168
- Space Group: P 21 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 61.903 | α = 90 |
| b = 144.605 | β = 90 |
| c = 49.612 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| PDB_EXTRACT | data extraction |
| MAR345dtb | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| AutoSol | phasing |
Entry History
Deposition Data
- Released Date: 2013-11-06 Deposition Author(s): Vorobiev, S., Lew, S., Seetharaman, J., Chi, Y., Xiao, R., Maglaqui, M., Lee, D., Everett, J.K., Acton, T.B., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium (NESG)
Revision History (Full details and data files)
- Version 1.0: 2013-11-06
Type: Initial release
