Download MendeleyThe crystal structure analysis of TM1154, oxidoreductase from Thermotoga maritima
Kim, Y., Joachimiak, A., Edwards, A., Skarina, T., Savchenko, A.To be published.
1PBT
The crystal structure of TM1154, oxidoreductase, sol/devB family from Thermotoga maritima
- PDB DOI: https://doi.org/10.2210/pdb1PBT/pdb
- Classification: HYDROLASE, OXIDOREDUCTASE
- Organism(s): Thermotoga maritima
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2003-05-15 Released: 2003-09-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.225
- R-Value Work: 0.179
- R-Value Observed: 0.179
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 |
| 6-phosphogluconolactonase | 244 | Thermotoga maritima | Mutation(s): 3 EC: 3.1.1.31 |  | |
UniProt | |||||
Find proteins for Q9X0N8 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)) Explore Q9X0N8 Go to UniProtKB: Q9X0N8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9X0N8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| TRS Query on TRS | D [auth A] | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL C4 H12 N O3 LENZDBCJOHFCAS-UHFFFAOYSA-O |  | ||
| SO4 Query on SO4 | B [auth A], C [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| EDO Query on EDO | E [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| FMT Query on FMT | F [auth A] | FORMIC ACID C H2 O2 BDAGIHXWWSANSR-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: 0.225
- R-Value Work: 0.179
- R-Value Observed: 0.179
- Space Group: C 2 2 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 37.729 | α = 90 |
| b = 75.084 | β = 90 |
| c = 148.252 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| d*TREK | data reduction |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| SOLVE | phasing |
| RESOLVE | phasing |
| ARP/wARP | model building |
Entry History
Deposition Data
- Released Date: 2003-09-23 Deposition Author(s): Kim, Y., Joachimiak, A., Edwards, A., Skarina, T., Savchenko, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2003-09-23
Type: Initial release - Version 1.1: 2008-04-29
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2024-11-20
Changes: Data collection, Database references, Derived calculations, Structure summary
