[English] 日本語
Yorodumi- PDB-2lep: Solution Structure of N-terminal Cytosolic Domain of Rhomboid Int... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2lep | ||||||
---|---|---|---|---|---|---|---|
Title | Solution Structure of N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Escherichia Coli | ||||||
Components | Rhomboid protease glpG 1 | ||||||
Keywords | HYDROLASE / Cell Membrane / Cytosol / Membrane Protein / Micelles / Serine Protease / Domain Swapping | ||||||
Function / homology | Function and homology information rhomboid protease / endopeptidase activity / membrane => GO:0016020 / serine-type endopeptidase activity / proteolysis / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Sherratt, A.R. / Ghasriani, H. / Goto, N.K. | ||||||
Citation | Journal: Biochemistry / Year: 2012 Title: Activity-Based Protein Profiling of the Escherichia coli GlpG Rhomboid Protein Delineates the Catalytic Core. Authors: Sherratt, A.R. / Blais, D.R. / Ghasriani, H. / Pezacki, J.P. / Goto, N.K. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2lep.cif.gz | 388.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2lep.ent.gz | 332.9 KB | Display | PDB format |
PDBx/mmJSON format | 2lep.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/le/2lep ftp://data.pdbj.org/pub/pdb/validation_reports/le/2lep | HTTPS FTP |
---|
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 7970.885 Da / Num. of mol.: 1 / Fragment: sequence database residues 1-61 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: glpG1, ECs4267 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / Variant (production host): DE3 References: UniProt: C3SPT7, UniProt: P09391*PLUS, rhomboid protease |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||
Sample conditions | Ionic strength: 0.30 M NaCl / pH: 6.5 / Pressure: ambient / Temperature: 298.15 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
---|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: molecular dynamics / Software ordinal: 1 / Details: Explicit solvent refinement. | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |