Download MendeleyThe structure of a putative Beta-galactosidase from Caulobacter crescentus CB15.
Cuff, M.E., Tesar, C., Clancy, S., Joachimiak, A.To be published.
3U7V
The structure of a putative Beta-galactosidase from Caulobacter crescentus CB15.
- PDB DOI: https://doi.org/10.2210/pdb3U7V/pdb
- Classification: HYDROLASE
- Organism(s): Caulobacter vibrioides NA1000
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2011-10-14 Released: 2011-12-21
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.215
- R-Value Work: 0.184
- R-Value Observed: 0.185
wwPDB Validation 3D Report Full Report
This is version 1.1 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 |
| Beta-galactosidase | 552 | Caulobacter vibrioides NA1000 | Mutation(s): 0 Gene Names: CCNA_00830, LacA EC: 3.2.1.23 |  | |
UniProt | |||||
Find proteins for A0A0H3C5N2 (Caulobacter vibrioides (strain NA1000 / CB15N)) Explore A0A0H3C5N2 Go to UniProtKB: A0A0H3C5N2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A0H3C5N2 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ACY Query on ACY | B [auth A], C [auth A] | ACETIC ACID C2 H4 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.215
- R-Value Work: 0.184
- R-Value Observed: 0.185
- Space Group: I 4
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 148.306 | α = 90 |
| b = 148.306 | β = 90 |
| c = 53.792 | γ = 90 |
| 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: 2011-12-21 Deposition Author(s): Cuff, M.E., Tesar, C., Clancy, S., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2011-12-21
Type: Initial release - Version 1.1: 2017-11-08
Changes: Refinement description
