Download MendeleyCrystal structure of Putative reductase (NP_038806.2) from MUS MUSCULUS at 1.18 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3LN3
Crystal structure of Putative reductase (NP_038806.2) from MUS MUSCULUS at 1.18 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3LN3/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Mus musculus
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2010-02-01 Released: 2010-02-16
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.18 Å
- R-Value Free: 0.156
- R-Value Work: 0.131
- R-Value Observed: 0.132
This is version 1.3 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 |
| Dihydrodiol dehydrogenase | 324 | Mus musculus | Mutation(s): 0 Gene Names: Akr1c13, ddh |  | |
UniProt | |||||
Find proteins for Q8VC28 (Mus musculus) Explore Q8VC28 Go to UniProtKB: Q8VC28 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8VC28 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAD Query on NAD | E [auth A] | NICOTINAMIDE-ADENINE-DINUCLEOTIDE C21 H27 N7 O14 P2 BAWFJGJZGIEFAR-NNYOXOHSSA-N |  | ||
| MRD Query on MRD | F [auth A] | (4R)-2-METHYLPENTANE-2,4-DIOL C6 H14 O2 SVTBMSDMJJWYQN-RXMQYKEDSA-N |  | ||
| SO4 Query on SO4 | B [auth A], C [auth A], D [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| Modified Residues 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MLY Query on MLY | A | L-PEPTIDE LINKING | C8 H18 N2 O2 |  | LYS |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.18 Å
- R-Value Free: 0.156
- R-Value Work: 0.131
- R-Value Observed: 0.132
- Space Group: C 1 2 1
- Diffraction Data: https://doi.org/10.18430/M33LN3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 157.506 | α = 90 |
| b = 47.206 | β = 94.98 |
| c = 47.1 | γ = 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: 2010-02-16 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2010-02-16
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2017-11-01
Changes: Refinement description - Version 1.3: 2019-07-17
Changes: Data collection, Derived calculations, Refinement description
