+Open data
-Basic information
Entry | Database: PDB / ID: 6p04 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Binary structure of the E52D mutant of ANT-4'' with Neomycin | |||||||||
Components | Kanamycin nucleotidyltransferase | |||||||||
Keywords | TRANSFERASE/ANTIBIOTIC / Aminoglycoside nucelotidyl transferase (ANT) / Aminoglycoside modifying enzymes (AGMEs) / DNA polymerase / ANTIBIOTIC / TRANSFERASE-ANTIBIOTIC complex | |||||||||
Function / homology | Function and homology information nucleotidyltransferase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / response to antibiotic Similarity search - Function | |||||||||
Biological species | Bacillus sp. (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | |||||||||
Authors | Selvaraj, B. / Cuneo, M.J. | |||||||||
Funding support | United States, 2items
| |||||||||
Citation | Journal: Acs Catalysis / Year: 2020 Title: "Catch and Release": a Variation of the Archetypal Nucleotidyl Transfer Reaction Authors: Selvaraj, B. / Kocaman, S. / Trifas, M. / Serpersu, E.H. / Cuneo, M.J. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 6p04.cif.gz | 122.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb6p04.ent.gz | 93.4 KB | Display | PDB format |
PDBx/mmJSON format | 6p04.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p0/6p04 ftp://data.pdbj.org/pub/pdb/validation_reports/p0/6p04 | HTTPS FTP |
---|
-Related structure data
Related structure data | 6p01C 6p06C 6p08C 1knyS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 29121.855 Da / Num. of mol.: 2 / Mutation: E52D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus sp. (bacteria) / Gene: knt, kan Production host: Escherichia coli-Pichia pastoris shuttle vector pPpARG4 (others) References: UniProt: P05058, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases #2: Chemical | #3: Chemical | ChemComp-MG / | #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.3 % |
---|---|
Crystal grow | Temperature: 285 K / Method: vapor diffusion, hanging drop / Details: 16% PEG 8K, 0.1 M Tris pH8.0, 0.1M MgCl2 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0332 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Dec 7, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→49.225 Å / Num. obs: 26344 / % possible obs: 98.4 % / Redundancy: 5.2 % / CC1/2: 0.954 / Rmerge(I) obs: 0.162 / Rpim(I) all: 0.104 / Rrim(I) all: 0.181 / Net I/σ(I): 5.5 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 5 % / Rmerge(I) obs: 0.644 / Mean I/σ(I) obs: 2.1 / Num. unique obs: 2530 / CC1/2: 0.697 / Rpim(I) all: 0.308 / Rrim(I) all: 0.716 / % possible all: 98.6 |
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1KNY Resolution: 2.3→49.225 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 25.69
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→49.225 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|