Download MendeleyThe structure of CysQ from Bacteroides thetaiotaomicron, a bacterial member of the inositol monophosphatase family.
Cuff, M.E., Mulligan, R., Abdullah, J., Joachimiak, A.To be published.
3B8B
Crystal structure of CysQ from Bacteroides thetaiotaomicron, a bacterial member of the inositol monophosphatase family
- PDB DOI: https://doi.org/10.2210/pdb3B8B/pdb
- Classification: HYDROLASE
- Organism(s): Bacteroides thetaiotaomicron VPI-5482
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2007-10-31 Released: 2007-12-18
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.188
- R-Value Work: 0.166
- R-Value Observed: 0.167
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 |
| CysQ, sulfite synthesis pathway protein | 292 | Bacteroides thetaiotaomicron VPI-5482 | Mutation(s): 0 Gene Names: cysQ, BT_0411 |  | |
UniProt | |||||
Find proteins for Q8AAQ3 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)) Explore Q8AAQ3 Go to UniProtKB: Q8AAQ3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8AAQ3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | B [auth A] C [auth A] D [auth A] E [auth A] F [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| CL Query on CL | H [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| Modified Residues 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| CSO Query on CSO | A | L-PEPTIDE LINKING | C3 H7 N O3 S |  | CYS |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.188
- R-Value Work: 0.166
- R-Value Observed: 0.167
- Space Group: P 61 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 93.927 | α = 90 |
| b = 93.927 | β = 90 |
| c = 140.783 | γ = 120 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| MLPHARE | phasing |
| DM | phasing |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
| SHELXD | phasing |
| SHELXE | model building |
| SOLVE | phasing |
| RESOLVE | phasing |
| ARP/wARP | model building |
| CCP4 | phasing |
| O | model building |
| Coot | model building |
Entry History
Deposition Data
- Released Date: 2007-12-18 Deposition Author(s): Cuff, M.E., Mulligan, R., Abdullah, J., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2007-12-18
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description
