Download MendeleyCrystal structure of the dipicolinate synthase chain B from Bacillus cereus.
Vorobiev, S., Lew, S., Abashidze, M., Seetharaman, J., Wang, H., Ciccosanti, C., Foote, E.L., Xiao, R., Acton, T.B., Montelione, G.T., Hunt, J.F., Tong, L.To be published.
3MCU
Crystal structure of the dipicolinate synthase chain B from Bacillus cereus. Northeast Structural Genomics Consortium Target BcR215.
- PDB DOI: https://doi.org/10.2210/pdb3MCU/pdb
- Classification: OXIDOREDUCTASE
- Organism(s): Bacillus cereus ATCC 14579
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2010-03-29 Released: 2010-04-14
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.30 Å
- R-Value Free: 0.241
- R-Value Work: 0.196
- R-Value Observed: 0.199
wwPDB Validation 3D Report Full Report
This is version 1.5 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 |
| Dipicolinate synthase, B chain | 207 | Bacillus cereus ATCC 14579 | Mutation(s): 0 Gene Names: BC_3800 |  | |
UniProt | |||||
Find proteins for Q819Z6 (Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)) Explore Q819Z6 Go to UniProtKB: Q819Z6 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q819Z6 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PO4 Query on PO4 | G [auth A] H [auth C] I [auth C] J [auth D] K [auth E] | PHOSPHATE ION O4 P NBIIXXVUZAFLBC-UHFFFAOYSA-K |  | ||
| 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 | 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: 0.241
- R-Value Work: 0.196
- R-Value Observed: 0.199
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 77.082 | α = 90 |
| b = 129.257 | β = 90 |
| c = 132.184 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| MOLREP | phasing |
| PHENIX | refinement |
| DENZO | data reduction |
| SCALEPACK | data scaling |
Entry History
Deposition Data
- Released Date: 2010-04-14 Deposition Author(s): Vorobiev, S., Lew, S., Abashidze, M., Seetharaman, J., Wang, H., Ciccosanti, C., Foote, E.L., Mao, L., Xiao, R., Acton, T.B., Montelione, G.T., Hunt, J.F., Tong, L., Northeast Structural Genomics Consortium (NESG)
Revision History (Full details and data files)
- Version 1.0: 2010-04-14
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2017-10-25
Changes: Author supporting evidence - Version 1.3: 2018-01-24
Changes: Structure summary - Version 1.4: 2023-09-06
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.5: 2023-11-22
Changes: Data collection
