Download MendeleyThe Active-Site Trimetallic Cluster of Alkaline Phosphatase is Lost Upon Isosteric Mutation at the Mg2+-Coordinating Residue Threonine-155
Grigg, J.C., Hucaluk, C., Murphy, M.E., Ritter, H., Yee, J., Rafferty, S.To be published.
3BDG
Crystal structure of wild-type/T155V mixed dimer of E. coli alkaline phosphatase
- PDB DOI: https://doi.org/10.2210/pdb3BDG/pdb
- Classification: HYDROLASE
- Organism(s): Escherichia coli
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2007-11-14 Released: 2008-11-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 Å
- R-Value Free: 0.180
- R-Value Work: 0.160
- R-Value Observed: 0.161
wwPDB Validation 3D Report Full Report
This is version 1.4 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 |
| Alkaline phosphatase | 458 | Escherichia coli | Mutation(s): 1 Gene Names: phoA EC: 3.1.3.1 |  | |
UniProt | |||||
Find proteins for P00634 (Escherichia coli (strain K12)) Explore P00634 Go to UniProtKB: P00634 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P00634 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Alkaline phosphatase | 458 | Escherichia coli | Mutation(s): 0 Gene Names: phoA EC: 3.1.3.1 |  | |
UniProt | |||||
Find proteins for P00634 (Escherichia coli (strain K12)) Explore P00634 Go to UniProtKB: P00634 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P00634 | ||||
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 B], E [auth B], F [auth B] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 Å
- R-Value Free: 0.180
- R-Value Work: 0.160
- R-Value Observed: 0.161
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 55.32 | α = 90 |
| b = 103.35 | β = 105.78 |
| c = 88.286 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| HKL-2000 | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2008-11-25 Deposition Author(s): Grigg, J.C., Murphy, M.E.
Revision History (Full details and data files)
- Version 1.0: 2008-11-25
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2012-09-19
Changes: Version format compliance - Version 1.3: 2021-10-20
Changes: Database references, Derived calculations - Version 1.4: 2023-08-30
Changes: Data collection, Refinement description
