|Entry||Database: PDB / ID: 2kud|
|Title||NMR structure of the PASTA domain 1 and 2 of Mycobacterium tuberculosis of PknB|
|Components||Serine/threonine-protein kinase pknB|
|Keywords||TRANSFERASE / kinase / external domain / signaling / STPK / resuscitation / Serine/threonine-protein kinase|
|Function / homology|
Function and homology information
negative regulation of growth rate / response to host immune response / acetyltransferase activator activity / negative regulation of fatty acid biosynthetic process / negative regulation of catalytic activity / positive regulation of catalytic activity / peptidoglycan biosynthetic process / peptidoglycan-based cell wall / protein serine/threonine/tyrosine kinase activity / positive regulation of DNA binding ...negative regulation of growth rate / response to host immune response / acetyltransferase activator activity / negative regulation of fatty acid biosynthetic process / negative regulation of catalytic activity / positive regulation of catalytic activity / peptidoglycan biosynthetic process / peptidoglycan-based cell wall / protein serine/threonine/tyrosine kinase activity / positive regulation of DNA binding / negative regulation of protein binding / manganese ion binding / regulation of cell shape / non-specific serine/threonine protein kinase / peptidyl-serine phosphorylation / protein kinase activity / protein autophosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / protein phosphorylation / membrane => GO:0016020 / ATP binding / metal ion binding / identical protein binding / plasma membrane / cytosol
Similarity search - Function
Trypsin Inhibitor V; Chain A - #20 / PASTA domain profile. / PASTA domain / PASTA domain / PASTA / Trypsin Inhibitor V; Chain A / Serine/Threonine protein kinases active-site signature. / Serine/threonine-protein kinase, active site / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain ...Trypsin Inhibitor V; Chain A - #20 / PASTA domain profile. / PASTA domain / PASTA domain / PASTA / Trypsin Inhibitor V; Chain A / Serine/Threonine protein kinases active-site signature. / Serine/threonine-protein kinase, active site / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Serine/threonine-protein kinase PknB / Serine/threonine-protein kinase PknB
Similarity search - Component
|Biological species||Mycobacterium tuberculosis (unknown)|
|Method||SOLUTION NMR / restrained molecular dynamics in a hydrated environment|
|Model details||lowest energy, model 1|
|Authors||Barthe, P. / Mukamolova, G. / Roumestand, C. / Cohen-Gonsaud, M.|
|Citation||Journal: Structure / Year: 2010|
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.
|Structure viewer||Molecule: |
Downloads & links
A: Serine/threonine-protein kinase pknB
|#1: Protein|| |
Mass: 14530.212 Da / Num. of mol.: 1 / Fragment: PASTA domains 1 and 2, residues 355-491
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (unknown) / Strain: H37Rv / Gene: Rv0014c / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P0A5S4, UniProt: P9WI81*PLUS, non-specific serine/threonine protein kinase
|Experiment||Method: SOLUTION NMR|
|Sample conditions||pH: 4.6 / Pressure: ambient / Temperature: 283 K|
|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
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