Download MendeleyCrystal structure of a putative oxidoreductase protein from Sinorhizobium meliloti 1021 in complex with NADP
Ghosh, A., Bhoshle, R., Toro, R., Gizzi, A., Hillerich, B., Seidel, R., Almo, S.C.To be published.
4ESO
Crystal structure of a putative oxidoreductase protein from Sinorhizobium meliloti 1021 in complex with NADP
- PDB DOI: https://doi.org/10.2210/pdb4ESO/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Sinorhizobium meliloti 1021
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2012-04-23 Released: 2012-05-16
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.91 Å
- R-Value Free: 0.234
- R-Value Work: 0.193
- R-Value Observed: 0.195
This is version 1.0 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 oxidoreductase | 255 | Sinorhizobium meliloti 1021 | Mutation(s): 0 Gene Names: R02322, SMc01571 EC: 1 |  | |
UniProt | |||||
Find proteins for Q92N93 (Rhizobium meliloti (strain 1021)) Explore Q92N93 Go to UniProtKB: Q92N93 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q92N93 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAP Query on NAP | E [auth A], F [auth B], H [auth C], J [auth D] | NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE C21 H28 N7 O17 P3 XJLXINKUBYWONI-NNYOXOHSSA-N |  | ||
| GOL Query on GOL | G [auth B], I [auth C] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C, D | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.91 Å
- R-Value Free: 0.234
- R-Value Work: 0.193
- R-Value Observed: 0.195
- Space Group: P 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 62.96 | α = 66.5 |
| b = 66.74 | β = 78.3 |
| c = 70.54 | γ = 62.96 |
| Software Name | Purpose |
|---|---|
| CBASS | data collection |
| SOLVE | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| SCALEPACK | data scaling |
Entry History
Deposition Data
- Released Date: 2012-05-16 Deposition Author(s): Ghosh, A., Bhoshle, R., Toro, R., Gizzi, A., Hillerich, B., Seidel, R., Almo, S.C., New York Structural Genomics Research Consortium (NYSGRC)
Revision History (Full details and data files)
- Version 1.0: 2012-05-16
Type: Initial release
