Download MendeleyUrea binding to guide rational design of mutations that influence enzyme dynamics
Hamill, C.J., Arcus, V.L., Prentice, E.J., Bahl, C., Truebridge, I.To be published.
7LV6 | pdb_00007lv6
The structure of MalL mutant enzyme S536R from Bacillus subtilis
- PDB DOI: https://doi.org/10.2210/pdb7LV6/pdb
- Classification: HYDROLASE
- Organism(s): Bacillus subtilis subsp. subtilis str. 168
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2021-02-24 Released: 2022-03-09
- Funding Organization(s): Marsden Fund
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.10 Å
- R-Value Free: 0.145 (Depositor), 0.145 (DCC)
- R-Value Work: 0.126 (Depositor), 0.128 (DCC)
- R-Value Observed: 0.127 (Depositor)
Starting Model: experimental
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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 |
| Oligo-1,6-glucosidase 1 | A [auth B] | 586 | Bacillus subtilis subsp. subtilis str. 168 | Mutation(s): 1 Gene Names: malL, yvdL, BSU34560 EC: 3.2.1.10 |  |
UniProt | |||||
Find proteins for O06994 (Bacillus subtilis (strain 168)) Explore O06994 Go to UniProtKB: O06994 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O06994 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| TRS Query on TRS | B | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL C4 H12 N O3 LENZDBCJOHFCAS-UHFFFAOYSA-O |  | ||
| GOL Query on GOL | C [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| CA Query on CA | D [auth B] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.10 Å
- R-Value Free: 0.145 (Depositor), 0.145 (DCC)
- R-Value Work: 0.126 (Depositor), 0.128 (DCC)
- R-Value Observed: 0.127 (Depositor)
Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 48.749 | α = 90 |
| b = 100.999 | β = 113.06 |
| c = 61.749 | γ = 90 |
| Software Name | Purpose |
|---|---|
| XDS | data reduction |
| Aimless | data scaling |
| MOLREP | phasing |
| REFMAC | refinement |
| PHENIX | refinement |
| Coot | model building |
| PDB_EXTRACT | data extraction |
Entry History & Funding Information
Deposition Data
- Released Date: 2022-03-09 Deposition Author(s): Hamill, C.J., Prentice, E.J., Bahl, C.D., Truebridge, I.S., Arcus, V.L.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Marsden Fund | New Zealand | 16-UOW-027 |
Revision History (Full details and data files)
- Version 1.0: 2022-03-09
Type: Initial release - Version 1.1: 2023-10-18
Changes: Data collection, Refinement description
