Download MendeleyCrystal structure of probable DsbA oxidoreductase SCO1869 from Streptomyces coelicolor
Chang, C., Xu, X., Cui, H., Savchenko, A., Edwards, A.M., Joachimiak, A.To be published.
3GL5 | pdb_00003gl5
Crystal structure of probable DsbA oxidoreductase SCO1869 from Streptomyces coelicolor
- PDB DOI: https://doi.org/10.2210/pdb3GL5/pdb
- Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
- Organism(s): Streptomyces coelicolor A3(2)
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-03-11 Released: 2009-03-31
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.15 Å
- R-Value Free: 0.246 (Depositor), 0.254 (DCC)
- R-Value Work: 0.200 (Depositor), 0.207 (DCC)
- R-Value Observed: 0.202 (Depositor)
wwPDB Validation 3D Report Full Report
This is version 1.2 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 DsbA oxidoreductase SCO1869 | 239 | Streptomyces coelicolor A3(2) | Mutation(s): 0 Gene Names: SCO1869, SCI39.16c |  | |
UniProt | |||||
Find proteins for Q93RV7 (Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)) Explore Q93RV7 Go to UniProtKB: Q93RV7 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q93RV7 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ACT Query on ACT | C [auth A] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| NA Query on NA | B [auth A] | SODIUM ION Na FKNQFGJONOIPTF-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: 2.15 Å
- R-Value Free: 0.246 (Depositor), 0.254 (DCC)
- R-Value Work: 0.200 (Depositor), 0.207 (DCC)
- R-Value Observed: 0.202 (Depositor)
Space Group: P 41 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 60.36 | α = 90 |
| b = 60.36 | β = 90 |
| c = 132.761 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| HKL-3000 | phasing |
| MLPHARE | phasing |
| DM | model building |
| SHELXD | phasing |
| RESOLVE | model building |
| ARP/wARP | model building |
| Coot | model building |
| REFMAC | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| DM | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2009-03-31 Deposition Author(s): Chang, C., Xu, X., Cui, H., Savchenko, A., Edwards, A.M., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-03-31
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Refinement description, Version format compliance - Version 1.2: 2024-11-06
Changes: Data collection, Database references, Derived calculations, Structure summary
