Download MendeleyCrystal structure of putative dinucleotide-binding oxidoreductase (NP_786167.1) from Lactobacillus plantarum at 1.60 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
2RAF
Crystal structure of putative dinucleotide-binding oxidoreductase (NP_786167.1) from Lactobacillus plantarum at 1.60 A resolution
- PDB DOI: https://doi.org/10.2210/pdb2RAF/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Lactiplantibacillus plantarum WCFS1
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2007-09-14 Released: 2007-10-02
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.60 Å
- R-Value Free: 0.186
- R-Value Work: 0.151
- R-Value Observed: 0.153
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 Dinucleotide-Binding Oxidoreductase | 209 | Lactiplantibacillus plantarum WCFS1 | Mutation(s): 0 Gene Names: NP_786167.1, lp_2792 EC: 1 |  | |
UniProt | |||||
Find proteins for F9URQ8 (Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)) Explore F9URQ8 Go to UniProtKB: F9URQ8 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | F9URQ8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAP Query on NAP | D [auth A] | NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE C21 H28 N7 O17 P3 XJLXINKUBYWONI-NNYOXOHSSA-N |  | ||
| PEG Query on PEG | E [auth C] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-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: 1.60 Å
- R-Value Free: 0.186
- R-Value Work: 0.151
- R-Value Observed: 0.153
- Space Group: C 2 2 21
- Diffraction Data: https://doi.org/10.18430/M32RAF
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 53.33 | α = 90 |
| b = 152.57 | β = 90 |
| c = 140.07 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SOLVE | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| XDS | data reduction |
Entry History
Deposition Data
- Released Date: 2007-10-02 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2007-10-02
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2017-10-25
Changes: Author supporting evidence, Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-01-25
Changes: Database references
