[English] 日本語
![](img/lk-miru.gif)
- PDB-2kue: NMR structure of the PASTA domain 2 and 3 of Mycobacterium tuberc... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2kue | ||||||
---|---|---|---|---|---|---|---|
Title | NMR structure of the PASTA domain 2 and 3 of Mycobacterium tuberculosis of PknB | ||||||
![]() | Serine/threonine-protein kinase pknB | ||||||
![]() | TRANSFERASE / kinase / external domain / signaling / STPK / resuscitation / Serine/threonine-protein kinase | ||||||
Function / homology | ![]() negative regulation of growth rate / acetyltransferase activator activity / negative regulation of catalytic activity / negative regulation of fatty acid biosynthetic process / response to host immune response / positive regulation of catalytic activity / positive regulation of DNA binding / peptidoglycan biosynthetic process / protein serine/threonine/tyrosine kinase activity / peptidoglycan-based cell wall ...negative regulation of growth rate / acetyltransferase activator activity / negative regulation of catalytic activity / negative regulation of fatty acid biosynthetic process / response to host immune response / positive regulation of catalytic activity / positive regulation of DNA binding / peptidoglycan biosynthetic process / protein serine/threonine/tyrosine kinase activity / peptidoglycan-based cell wall / negative regulation of protein binding / manganese ion binding / regulation of cell shape / protein autophosphorylation / membrane => GO:0016020 / non-specific serine/threonine protein kinase / protein kinase activity / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / identical protein binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / restrained molecular dynamics in a hydrated environment | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Barthe, P. / Mukamolova, G. / Roumestand, C. / Cohen-Gonsaud, M. | ||||||
![]() | ![]() Title: The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation Authors: Barthe, P. / Mukamolova, G.V. / Roumestand, C. / Cohen-Gonsaud, M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 1.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 544.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 794.3 KB | Display | |
Data in XML | ![]() | 73 KB | Display | |
Data in CIF | ![]() | 114.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2kudC ![]() 2kufC ![]() 2kuiC C: citing same article ( |
---|---|
Similar structure data | |
Other databases |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 14238.938 Da / Num. of mol.: 1 / Fragment: PASTA domains 2 and 3, RESIDUES 423-557 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0A5S4, UniProt: P9WI81*PLUS, non-specific serine/threonine protein kinase |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||||||
Sample conditions | pH: 4.6 / Pressure: ambient / Temperature: 283 K |
-NMR measurement
NMR spectrometer |
|
---|
-
Processing
NMR software | Name: CNS / Version: 1.2 / Classification: refinement |
---|---|
Refinement | Method: restrained molecular dynamics in a hydrated environment Software ordinal: 1 / Details: like RECOORD database |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 30 / Representative conformer: 1 |