Download MendeleyStructural and functional characterization of the scoulerine 9-O methyltransferase from Thalictrum flavum.
Valentic, T.R., Smolke, C.S., Payne, J.T.To be published.
6NEJ
scoulerine 9-O-methyltransferase from Thalictrum flavum complexed (13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol and with S-ADENOSYL-L-HOMOCYSTEINE
- PDB DOI: https://doi.org/10.2210/pdb6NEJ/pdb
- Classification: BIOSYNTHETIC PROTEIN
- Organism(s): Thalictrum flavum subsp. glaucum
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2018-12-17 Released: 2019-12-18
- Funding Organization(s): National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.60 ?
- R-Value Free: 0.205
- R-Value Work: 0.183
- R-Value Observed: 0.183
Starting Model: experimental
View more details
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 |
| (S)-scoulerine 9-O-methyltransferase | 375 | Thalictrum flavum subsp. glaucum | Mutation(s): 0 EC: 2.1.1.117 |  | |
UniProt | |||||
Find proteins for Q5C9L2 (Thalictrum flavum subsp. glaucum) Explore Q5C9L2 Go to UniProtKB: Q5C9L2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5C9L2 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SAH Query on SAH | D [auth A], F [auth B] | S-ADENOSYL-L-HOMOCYSTEINE C14 H20 N6 O5 S ZJUKTBDSGOFHSH-WFMPWKQPSA-N |  | ||
| SLX Query on SLX | C [auth A], E [auth B] | (13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol C19 H21 N O4 KNWVMRVOBAFFMH-HNNXBMFYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.60 ?
- R-Value Free: 0.205
- R-Value Work: 0.183
- R-Value Observed: 0.183
- Space Group: P 1 21 1
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 61.635 | ¦Á = 90 |
| b = 70.775 | ¦Â = 94.35 |
| c = 67.365 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| iMOSFLM | data reduction |
| Aimless | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2019-12-18 Deposition Author(s): Valentic, T.R., Smolke, C.D., Payne, J.T.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI) | United States | DP1AT007886-05 |
Revision History (Full details and data files)
- Version 1.0: 2019-12-18
Type: Initial release - Version 1.1: 2024-03-13
Changes: Data collection, Database references - Version 1.2: 2024-04-03
Changes: Refinement description
