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- PDB-1urf: HR1b domain from PRK1 -

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Basic information

Entry
Database: PDB / ID: 1urf
TitleHR1b domain from PRK1
ComponentsPROTEIN KINASE C-LIKE 1
KeywordsTRANSFERASE / G-PROTEIN / HR1 DOMAIN / KINASE / HELICAL / COILED COIL / ATP-BINDING / SERINE/THREONINE-PROTEIN KINASE / PHOSPHORYLATION
Function / homology
Function and homology information


epithelial cell migration / protein kinase C / diacylglycerol-dependent serine/threonine kinase activity / renal system process / regulation of germinal center formation / B cell apoptotic process / histone H3T11 kinase activity / hyperosmotic response / regulation of cell motility / regulation of androgen receptor signaling pathway ...epithelial cell migration / protein kinase C / diacylglycerol-dependent serine/threonine kinase activity / renal system process / regulation of germinal center formation / B cell apoptotic process / histone H3T11 kinase activity / hyperosmotic response / regulation of cell motility / regulation of androgen receptor signaling pathway / regulation of immunoglobulin production / nuclear androgen receptor binding / RHOB GTPase cycle / RHOC GTPase cycle / negative regulation of B cell proliferation / cleavage furrow / B cell homeostasis / RHOA GTPase cycle / RHO GTPases activate PKNs / spleen development / RAC1 GTPase cycle / post-translational protein modification / protein kinase C binding / nuclear receptor coactivator activity / negative regulation of protein phosphorylation / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / small GTPase binding / histone deacetylase binding / midbody / histone binding / endosome / protein kinase activity / intracellular signal transduction / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / chromatin binding / regulation of transcription by RNA polymerase II / signal transduction / protein-containing complex / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Serine/threonine-protein kinase N1, second HR1 domain / HR1 repeat / Serine/threonine-protein kinase N, first HR1 domain / Serine/threonine-protein kinase N, C2 domain / Hr1 repeat / Rho effector or protein kinase C-related kinase homology region 1 homologues / HR1 repeat superfamily / HR1 rho-binding domain / REM-1 domain profile. / Protein kinase, C-terminal ...Serine/threonine-protein kinase N1, second HR1 domain / HR1 repeat / Serine/threonine-protein kinase N, first HR1 domain / Serine/threonine-protein kinase N, C2 domain / Hr1 repeat / Rho effector or protein kinase C-related kinase homology region 1 homologues / HR1 repeat superfamily / HR1 rho-binding domain / REM-1 domain profile. / Protein kinase, C-terminal / Protein kinase C terminal domain / C2 domain / C2 domain profile. / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / C2 domain superfamily / Helix Hairpins / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / 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 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Serine/threonine-protein kinase N1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsOwen, D. / Lowe, P.N. / Nietlispach, D. / Brosnan, C.E. / Chirgadze, D.Y. / Parker, P.J. / Blundell, T.L. / Mott, H.R.
CitationJournal: J.Biol.Chem. / Year: 2003
Title: Molecular Dissection of the Interaction between the Small G Proteins Rac1 and Rhoa and Protein Kinase C-Related Kinase 1 (Prk1)
Authors: Owen, D. / Lowe, P.N. / Nietlispach, D. / Brosnan, C.E. / Chirgadze, D.Y. / Parker, P.J. / Blundell, T.L. / Mott, H.R.
History
DepositionOct 29, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 6, 2003Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PROTEIN KINASE C-LIKE 1


Theoretical massNumber of molelcules
Total (without water)9,0171
Polymers9,0171
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)24 / 100LOWEST ENERGY
RepresentativeModel #17

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Components

#1: Protein PROTEIN KINASE C-LIKE 1 / PLK1_HUMAN / PROTEIN-KINASE C-RELATED KINASE 1 / PROTEIN KINASE C-LIKE PKN / SERINE-THREONINE PROTEIN KINASE N


Mass: 9017.416 Da / Num. of mol.: 1 / Fragment: HR1B, RESIDUES 122-199
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX-3X / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21
References: UniProt: Q16512, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor
Compound detailsFUNCTION: PHOSPHORYLATES RIBOSOMAL PROTEIN S6. MEDIATES GTPASE RHO DEPENDENT INTRACELLULAR ...FUNCTION: PHOSPHORYLATES RIBOSOMAL PROTEIN S6. MEDIATES GTPASE RHO DEPENDENT INTRACELLULAR SIGNALLING ENZYME REGULATION:

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N-HSQC
12113C-HSQC
13115N-NOESY
14115N-TOCSY
151HN(CA)CB
161(H)CCH-TOCSY
17113C-NOESY
181HNCA
191HN(CO)CA
1101CBCA(CO)NH
1111H(CC)(CO)NH

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Sample preparation

Sample conditionsIonic strength: 60 mM / pH: 7.4 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CNS1BRUNGERrefinement
AZARAstructure solution
ANSIGstructure solution
CNSstructure solution
ARIAstructure solution
RefinementMethod: torsion angle dynamics / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 24

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