Download MendeleyCrystal structure of a dihydrolipoamide dehydrogenase from Sinorhizobium meliloti 1021
Kumaran, D., Almo, S.C., Swaminathan, S.To be published.
3URH
Crystal structure of a dihydrolipoamide dehydrogenase from Sinorhizobium meliloti 1021
- PDB DOI: https://doi.org/10.2210/pdb3URH/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Sinorhizobium meliloti 1021
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2011-11-22 Released: 2011-12-14
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.227
- R-Value Work: 0.184
- R-Value Observed: 0.186
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 |
| Dihydrolipoyl dehydrogenase | 491 | Sinorhizobium meliloti 1021 | Mutation(s): 0 Gene Names: lpdA2, R03048, SMc02487 EC: 1.8.1.4 |  | |
UniProt | |||||
Find proteins for Q92LK0 (Rhizobium meliloti (strain 1021)) Explore Q92LK0 Go to UniProtKB: Q92LK0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q92LK0 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FAD Query on FAD | C [auth A], E [auth B] | FLAVIN-ADENINE DINUCLEOTIDE C27 H33 N9 O15 P2 VWWQXMAJTJZDQX-UYBVJOGSSA-N |  | ||
| SO4 Query on SO4 | D [auth A], F [auth B] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| EDO Query on EDO | G [auth B] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.227
- R-Value Work: 0.184
- R-Value Observed: 0.186
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 74.433 | α = 90 |
| b = 104.716 | β = 90 |
| c = 120.622 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CBASS | data collection |
| SHELXD | phasing |
| SHELXE | model building |
| ARP/wARP | model building |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2011-12-14 Deposition Author(s): Kumaran, D., Chamala, S., Evans, B., Foti, R., Gizzi, A., Hillerich, B., Kar, A., LaFleur, J., Seidel, R., Villigas, G., Zencheck, W., Almo, S.C., Swaminathan, S., New York Structural Genomics Research Consortium (NYSGRC)
Revision History (Full details and data files)
- Version 1.0: 2011-12-14
Type: Initial release
