Download MendeleyThe crystal structure of a thioesteras from Actinomadura verrucosospora.
Tan, K., Joachimiak, G., Endres, M., Phillips Jr., G.N., Joachmiak, A.To be published.
5VPJ
The crystal structure of a thioesteras from Actinomadura verrucosospora.
- PDB DOI: https://doi.org/10.2210/pdb5VPJ/pdb
- Classification: HYDROLASE
- Organism(s): Actinomadura verrucosospora
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2017-05-05 Released: 2017-07-19
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS), Department of Energy (DOE, United States)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.35 Å
- R-Value Free: 0.227
- R-Value Work: 0.186
- R-Value Observed: 0.188
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 |
| Thioesterase | 159 | Actinomadura verrucosospora | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for A0A2D0TCG5 (Actinomadura verrucosospora) Explore A0A2D0TCG5 Go to UniProtKB: A0A2D0TCG5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A2D0TCG5 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PG4 Query on PG4 | N [auth D] | TETRAETHYLENE GLYCOL C8 H18 O5 UWHCKJMYHZGTIT-UHFFFAOYSA-N |  | ||
| CL Query on CL | M [auth A], O [auth G], P [auth H], Q [auth K], R [auth K] | 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, E A, B, C, D, E, F, G, H, I, J, K, L | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.35 Å
- R-Value Free: 0.227
- R-Value Work: 0.186
- R-Value Observed: 0.188
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 105.68 | α = 90 |
| b = 96.358 | β = 99.16 |
| c = 114.16 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2017-07-19 Deposition Author(s): Tan, K., Joachimiak, G., Endres, M., Phillips Jr., G.N., Joachmiak, A., Midwest Center for Structural Genomics (MCSG), Enzyme Discovery for Natural Product Biosynthesis (NatPro)
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | GN094586, GM115585 |
| Department of Energy (DOE, United States) | United States | DE-AC02-06CH11357 |
Revision History (Full details and data files)
- Version 1.0: 2017-07-19
Type: Initial release - Version 1.1: 2017-09-13
Changes: Author supporting evidence - Version 1.2: 2019-12-04
Changes: Author supporting evidence
