Download MendeleyCrystal structure of enoyl-CoA hydrotase from Deinococcus radiodurans R1
Eswaramoorthy, S., Almo, S.C., Swaminathan, S.To be published.
4JOT
Crystal structure of enoyl-CoA hydrotase from Deinococcus radiodurans R1
- PDB DOI: https://doi.org/10.2210/pdb4JOT/pdb
- Classification: LYASE
- Organism(s): Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2013-03-18 Released: 2013-04-17
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.94 Å
- R-Value Free: 0.220
- R-Value Work: 0.193
- R-Value Observed: 0.194
wwPDB Validation 3D Report Full Report
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 |
| Enoyl-CoA hydratase, putative | 279 | Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 | Mutation(s): 0 Gene Names: DR_0114 |  | |
UniProt | |||||
Find proteins for Q9RY37 (Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)) Explore Q9RY37 Go to UniProtKB: Q9RY37 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9RY37 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | B [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.94 Å
- R-Value Free: 0.220
- R-Value Work: 0.193
- R-Value Observed: 0.194
- Space Group: I 2 3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 117.892 | α = 90 |
| b = 117.892 | β = 90 |
| c = 117.892 | γ = 90 |
| Software Name | Purpose |
|---|---|
| CBASS | data collection |
| SHELXS | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2013-04-17 Deposition Author(s): Eswaramoorthy, S., Chamala, S., Evans, B., Foti, F., Gizzi, A., Hillerich, B., Kar, A., Lafleur, J., Seidel, R., Villigas, G., Zencheck, W., Al Obaidi, N., Almo, S.C., Swaminathan, S., New York Structural Genomics Research Consortium (NYSGRC)
Revision History (Full details and data files)
- Version 1.0: 2013-04-17
Type: Initial release
