Download MendeleyCrystal structure of Putative anti-sigma factor antagonist TM1081 (TM1081) from THERMOTOGA MARITIMA at 1.59 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3F43
Crystal structure of a putative anti-sigma factor antagonist (tm1081) from thermotoga maritima at 1.59 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3F43/pdb
- Classification: TRANSCRIPTION
- Organism(s): Thermotoga maritima
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-10-31 Released: 2008-11-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.59 Å
- R-Value Free: 0.209
- R-Value Work: 0.178
- R-Value Observed: 0.179
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 |
| Putative anti-sigma factor antagonist TM1081 | 125 | Thermotoga maritima | Mutation(s): 0 Gene Names: TM1081, TM_1081 |  | |
UniProt | |||||
Find proteins for Q9X0H0 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)) Explore Q9X0H0 Go to UniProtKB: Q9X0H0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9X0H0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 1PE Query on 1PE | E [auth A] | PENTAETHYLENE GLYCOL C10 H22 O6 JLFNLZLINWHATN-UHFFFAOYSA-N |  | ||
| PEG Query on PEG | F [auth A] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
| CL Query on CL | B [auth A], C [auth A], D [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-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: 1.59 Å
- R-Value Free: 0.209
- R-Value Work: 0.178
- R-Value Observed: 0.179
- Space Group: P 41 21 2
- Diffraction Data: https://doi.org/10.18430/M33F43
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 49.7 | α = 90 |
| b = 49.7 | β = 90 |
| c = 113.62 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SOLVE | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| XDS | data reduction |
Entry History
Deposition Data
- Released Date: 2008-11-25 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-11-25
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: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations
