Download MendeleyCrystal structure of myo-inositol 2-dehydrogenase (NP_786804.1) from Lactobacillus plantarum at 2.40 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3CEA
Crystal structure of myo-inositol 2-dehydrogenase (NP_786804.1) from Lactobacillus plantarum at 2.40 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3CEA/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Lactiplantibacillus plantarum WCFS1
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-02-28 Released: 2008-03-11
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.40 Å
- R-Value Free: 0.243
- R-Value Work: 0.193
- R-Value Observed: 0.196
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 |
| Myo-inositol 2-dehydrogenase | 346 | Lactiplantibacillus plantarum WCFS1 | Mutation(s): 0 Gene Names: NP_786804.1, iolG1, lp_3605 EC: 1.1.1.18 |  | |
UniProt | |||||
Find proteins for F9ULF9 (Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)) Explore F9ULF9 Go to UniProtKB: F9ULF9 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | F9ULF9 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAD Query on NAD | E [auth A], G [auth B], H [auth C], J [auth D] | NICOTINAMIDE-ADENINE-DINUCLEOTIDE C21 H27 N7 O14 P2 BAWFJGJZGIEFAR-NNYOXOHSSA-N |  | ||
| EDO Query on EDO | I [auth C], K [auth D], L [auth D] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| CL Query on CL | F [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| 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: 2.40 Å
- R-Value Free: 0.243
- R-Value Work: 0.193
- R-Value Observed: 0.196
- Space Group: P 1 21 1
- Diffraction Data: https://doi.org/10.18430/M33CEA
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 47.331 | α = 90 |
| b = 145.684 | β = 91.92 |
| c = 100.208 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| SCALA | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| MOSFLM | data reduction |
| SHELXD | phasing |
| SHARP | phasing |
Entry History
Deposition Data
- Released Date: 2008-03-11 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-03-11
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations
