Download MendeleyNortheast Structural Genomics Consortium Target HR487
Kuzin, A., Su, M., Seetharaman, J., Patel, P., Xiao, R., Ciccosanti, C., Shastry, R., Everett, J.K., Nair, R., Acton, T.B., Rost, B., Montelione, G.T., Tong, L., Hunt, J.F.To be published.
3RQS
Crystal Structure of human L-3- Hydroxyacyl-CoA dehydrogenase (EC1.1.1.35) from mitochondria at the resolution 2.0 A, Northeast Structural Genomics Consortium Target HR487, Mitochondrial Protein Partnership
- PDB DOI: https://doi.org/10.2210/pdb3RQS/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2011-04-28 Released: 2011-05-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.204
- R-Value Work: 0.166
- R-Value Observed: 0.168
wwPDB Validation 3D Report Full Report
This is version 1.5 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 |
| Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial | 324 | Homo sapiens | Mutation(s): 1 Gene Names: HADH, HAD, HADHSC, SCHAD EC: 1.1.1.35 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q16836 (Homo sapiens) Explore Q16836 Go to UniProtKB: Q16836 | |||||
PHAROS: Q16836 GTEx: ENSG00000138796 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q16836 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | C [auth A] D [auth A] E [auth A] F [auth A] G [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-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: 2.00 Å
- R-Value Free: 0.204
- R-Value Work: 0.166
- R-Value Observed: 0.168
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 49.691 | α = 90 |
| b = 85.761 | β = 90 |
| c = 165.614 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| PDB_EXTRACT | data extraction |
| ADSC | data collection |
| HKL-2000 | data reduction |
| SCALEPACK | data scaling |
| BALBES | phasing |
Entry History
Deposition Data
- Released Date: 2011-05-25 Deposition Author(s): Kuzin, A., Su, M., Seetharaman, J., Patel, P., Xiao, R., Ciccosanti, C., Shastry, R., Everett, J.K., Nair, R., Acton, T.B., Rost, B., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium (NESG), Mitochondrial Protein Partnership (MPP)
Revision History (Full details and data files)
- Version 1.0: 2011-05-25
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2011-07-27
Changes: Structure summary - Version 1.3: 2011-08-03
Changes: Structure summary - Version 1.4: 2023-09-13
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.5: 2023-12-06
Changes: Data collection
