Download MendeleyCrystal structure of Putative bacterial transcription regulation protein (NP_372959.1) from Staphylococcus aureus MU50 at 1.81 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3LUR
Crystal structure of Putative bacterial transcription regulation protein (NP_372959.1) from Staphylococcus aureus MU50 at 1.81 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3LUR/pdb
- Classification: Transcription activator
- Organism(s): Staphylococcus aureus subsp. aureus Mu50
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2010-02-18 Released: 2010-03-09
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.81 ?
- R-Value Free: 0.218
- R-Value Work: 0.176
- R-Value Observed: 0.178
wwPDB Validation 3D Report Full Report
This is version 1.5 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 bacterial transcription regulation protein | 158 | Staphylococcus aureus subsp. aureus Mu50 | Mutation(s): 0 Gene Names: SAV2435 |  | |
UniProt | |||||
Find proteins for A0A0H3K0Y5 (Staphylococcus aureus (strain Mu50 / ATCC 700699)) Explore A0A0H3K0Y5 Go to UniProtKB: A0A0H3K0Y5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A0H3K0Y5 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PG4 Query on PG4 | D [auth A] | TETRAETHYLENE GLYCOL C8 H18 O5 UWHCKJMYHZGTIT-UHFFFAOYSA-N |  | ||
| PEG Query on PEG | J [auth B] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
| EDO Query on EDO | E [auth A] F [auth A] G [auth A] H [auth A] I [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.81 ?
- R-Value Free: 0.218
- R-Value Work: 0.176
- R-Value Observed: 0.178
- Space Group: P 1 21 1
- Diffraction Data: https://doi.org/10.18430/M33LUR
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 34.179 | ¦Á = 90 |
| b = 62.482 | ¦Â = 93.33 |
| c = 105.075 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| XDS | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2010-03-09 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2010-03-09
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-11-08
Changes: Refinement description - Version 1.3: 2019-07-17
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations - Version 1.5: 2024-10-30
Changes: Data collection, Refinement description, Structure summary
