Download MendeleyNortheast Structural Genomics Consortium Target BcR20
Forouhar, F., Neely, H., Seetharaman, J., Ciano, C., Ma, L., Zhao, L., Everett, J.K., Nair, R., Acton, T.B., Rost, B., Montelione, G.T., Tong, L., Hunt, J.F.To be published.
3GU3
Crystal Structure of the methyltransferase BC_2162 in complex with S-Adenosyl-L-Homocysteine from Bacillus cereus, Northeast Structural Genomics Consortium Target BcR20
- PDB DOI: https://doi.org/10.2210/pdb3GU3/pdb
- Classification: TRANSFERASE
- Organism(s): Bacillus cereus ATCC 14579
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-03-28 Released: 2009-04-07
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.212
- R-Value Work: 0.184
- R-Value Observed: 0.185
This is version 1.4 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 |
| Methyltransferase | 284 | Bacillus cereus ATCC 14579 | Mutation(s): 0 Gene Names: BC_2162 EC: 2.1.1 |  | |
UniProt | |||||
Find proteins for Q81E32 (Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)) Explore Q81E32 Go to UniProtKB: Q81E32 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q81E32 | ||||
Sequence AnnotationsExpand | |||||
| |||||
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 |  | ||
| ACT Query on ACT | C [auth A], E [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 | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.212
- R-Value Work: 0.184
- R-Value Observed: 0.185
- Space Group: P 32
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 90.793 | α = 90 |
| b = 90.793 | β = 90 |
| c = 122.627 | γ = 120 |
| Software Name | Purpose |
|---|---|
| CNS | refinement |
| PDB_EXTRACT | data extraction |
| ADSC | data collection |
| HKL-2000 | data reduction |
| SCALEPACK | data scaling |
| SnB | phasing |
| REFMAC | refinement |
Entry History
Deposition Data
- Released Date: 2009-04-07 Deposition Author(s): Forouhar, F., Neely, H., Seetharaman, J., Ciano, C., Ma, L., Zhao, L., Everett, J.K., Nair, R., Acton, T.B., Rost, B., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium (NESG)
Revision History (Full details and data files)
- Version 1.0: 2009-04-07
Type: Initial release - Version 1.1: 2011-07-13
Changes: Source and taxonomy, Version format compliance - Version 1.2: 2011-08-24
Changes: Structure summary - Version 1.3: 2017-11-01
Changes: Refinement description - Version 1.4: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description
