Download MendeleyCrystal Structure of BES from Bacillus cereus.
Kim, Y., Maltseva, N., Zawadzka, A., Holzle, D., Joachimiak, A.To be published.
2QM0 | pdb_00002qm0
Crystal structure of BES protein from Bacillus cereus
- PDB DOI: https://doi.org/10.2210/pdb2QM0/pdb
- Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
- Organism(s): Bacillus cereus ATCC 14579
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2007-07-13 Released: 2007-07-31
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.84 Å
- R-Value Free: 0.228 (Depositor), 0.244 (DCC)
- R-Value Work: 0.184 (Depositor), 0.201 (DCC)
- R-Value Observed: 0.189 (Depositor)
wwPDB Validation 3D Report Full Report
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 |
| BES | 275 | Bacillus cereus ATCC 14579 | Mutation(s): 4 Gene Names: BC_3734 |  | |
UniProt | |||||
Find proteins for Q81A57 (Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)) Explore Q81A57 Go to UniProtKB: Q81A57 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q81A57 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | C [auth A], D [auth A], E [auth B], F [auth B], G [auth B] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| Modified Residues 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
| SVY Query on SVY | A, B | L-PEPTIDE LINKING | C9 H20 N O6 P |  | SER |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.84 Å
- R-Value Free: 0.228 (Depositor), 0.244 (DCC)
- R-Value Work: 0.184 (Depositor), 0.201 (DCC)
- R-Value Observed: 0.189 (Depositor)
Space Group: C 2 2 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 48.849 | α = 90 |
| b = 135.058 | β = 90 |
| c = 200.873 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| SBC-Collect | data collection |
| HKL-3000 | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
| SHELXD | phasing |
| SHELXE | model building |
| MLPHARE | phasing |
| DM | phasing |
| SOLVE | phasing |
| RESOLVE | phasing |
| CCP4 | phasing |
| ARP/wARP | model building |
| O | model building |
| Coot | model building |
Entry History
Deposition Data
- Released Date: 2007-07-31 Deposition Author(s): Kim, Y., Maltseva, N., Zawadzka, A., Holzle, D., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2007-07-31
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2025-03-26
Changes: Data collection, Database references, Derived calculations, Structure summary
