Download MendeleyThe crystal structure of enoyl-CoA hydratase from Mycobacterium tuberculosis H37Rv
Tan, K., Holowicki, J., Endres, M., Kim, C.-Y., Kim, H., Hung, L.-W., Terwilliger, T.C., Joachimiak, A.To be published.
4JJT
The crystal structure of enoyl-CoA hydratase from Mycobacterium tuberculosis H37Rv
- PDB DOI: https://doi.org/10.2210/pdb4JJT/pdb
- Classification: LYASE
- Organism(s): Mycobacterium tuberculosis H37Rv
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2013-03-08 Released: 2013-03-27
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.227
- R-Value Work: 0.180
- R-Value Observed: 0.182
wwPDB Validation 3D Report Full Report
This is version 1.2 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 | 252 | Mycobacterium tuberculosis H37Rv | Mutation(s): 0 Gene Names: Mycobacterium tuberculosis, RVBD_2831 EC: 4.2.1.17 |  | |
UniProt | |||||
Find proteins for I6YEH6 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)) Explore I6YEH6 Go to UniProtKB: I6YEH6 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | I6YEH6 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | D [auth A], E [auth B], G [auth C] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | F [auth B] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.227
- R-Value Work: 0.180
- R-Value Observed: 0.182
- Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 130.318 | α = 90 |
| b = 86.874 | β = 126.02 |
| c = 80.957 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| MOLREP | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
Entry History
Deposition Data
- Released Date: 2013-03-27 Deposition Author(s): Tan, K., Holowicki, J., Endres, M., Kim, C.-Y., Kim, H., Hung, L.-W., Terwilliger, T.C., Joachimiak, A., Midwest Center for Structural Genomics (MCSG), Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors (MTBI)
Revision History (Full details and data files)
- Version 1.0: 2013-03-27
Type: Initial release - Version 1.1: 2023-09-20
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.2: 2023-12-06
Changes: Data collection
