Download MendeleyControl and regulation of S-Adenosylmethionine biosynthesis by the regulatory beta subunit and quinolone-based compounds
Panmanee, J., Bradley-Clarke, J., Mato, J.M., O'Neill, P.M., Antonyuk, S.V., Hasnain, S.S.(2020) FEBS J
6FAJ | pdb_00006faj
The structure of Human Methionine Adenosyltransferase II in apo state
- PDB DOI: https://doi.org/10.2210/pdb6FAJ/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2017-12-15 Released: 2019-02-06
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 ?
- R-Value Free: 0.224 (Depositor), 0.230 (DCC)
- R-Value Work: 0.190 (Depositor), 0.200 (DCC)
- R-Value Observed: 0.191 (Depositor)
Starting Model: experimental
View more details
wwPDB Validation 3D Report Full Report
This is version 1.2 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| S-adenosylmethionine synthase isoform type-2 | 395 | Homo sapiens | Mutation(s): 0 Gene Names: MAT2A, AMS2, MATA2 EC: 2.5.1.6 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P31153 (Homo sapiens) Explore P31153 Go to UniProtKB: P31153 | |||||
PHAROS: P31153 GTEx: ENSG00000168906 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P31153 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PG4 Query on PG4 | D [auth A] | TETRAETHYLENE GLYCOL C8 H18 O5 UWHCKJMYHZGTIT-UHFFFAOYSA-N |  | ||
| PEG Query on PEG | C [auth A], F [auth B] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | E [auth A] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 ?
- R-Value Free: 0.224 (Depositor), 0.230 (DCC)
- R-Value Work: 0.190 (Depositor), 0.200 (DCC)
- R-Value Observed: 0.191 (Depositor)
Space Group: P 2 21 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 62.176 | α = 90 |
| b = 103.232 | β = 90 |
| c = 108.359 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| iMOSFLM | data reduction |
| Aimless | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2019-02-06 Deposition Author(s): Bradley-Clarke, J., Panmanee, J., Antonyuk, S.V., Hasnain, S.S.
Revision History (Full details and data files)
- Version 1.0: 2019-02-06
Type: Initial release - Version 1.1: 2020-08-19
Changes: Database references - Version 1.2: 2024-01-17
Changes: Data collection, Database references, Refinement description
