Download MendeleyStructure and Function of Terfestatin Biosynthesis Enzymes TerB and TerC
Clinger, J.A., Elshahawi, S.I., Zhang, Y., Hall, R.P., Liu, Y., Miller, M.D., Thorson, J.S., Phillips Jr., G.N.To be published.
6D2V
Apo Structure of TerB, an NADP Dependent Oxidoreductase in the Terfestatin Biosynthesis Pathway
- PDB DOI: https://doi.org/10.2210/pdb6D2V/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Streptomyces
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2018-04-14 Released: 2018-06-13
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS), National Institutes of Health/National Cancer Institute (NIH/NCI)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.198
- R-Value Work: 0.161
- R-Value Observed: 0.163
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 |
| TerB Oxidoreductase | 315 | Streptomyces | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for A0A3B6UEU0 (Streptomyces) Explore A0A3B6UEU0 Go to UniProtKB: A0A3B6UEU0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A3B6UEU0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NDP (Subject of Investigation/LOI) Query on NDP | C [auth A], G [auth B] | NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE C21 H30 N7 O17 P3 ACFIXJIJDZMPPO-NNYOXOHSSA-N |  | ||
| SCN Query on SCN | D [auth A], H [auth B], I [auth B] | THIOCYANATE ION C N S ZMZDMBWJUHKJPS-UHFFFAOYSA-M |  | ||
| CL Query on CL | E [auth A], F [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.198
- R-Value Work: 0.161
- R-Value Observed: 0.163
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 58.516 | α = 90 |
| b = 80.598 | β = 90 |
| c = 139.518 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XDS | data reduction |
| XDS | data scaling |
| PDB_EXTRACT | data extraction |
| PHENIX | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2018-06-13 Deposition Author(s): Clinger, J.A., Elshahawi, S.I., Zhang, Y., Hall, R.P., Liu, Y., Thorson, J.S., Phillips Jr., G.N.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | -- |
| National Institutes of Health/National Cancer Institute (NIH/NCI) | United States | -- |
Revision History (Full details and data files)
- Version 1.0: 2018-06-13
Type: Initial release - Version 1.1: 2019-12-04
Changes: Author supporting evidence - Version 1.2: 2024-03-13
Changes: Data collection, Database references, Refinement description
