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- PDB-1bl6: THE COMPLEX STRUCTURE OF THE MAP KINASE P38/SB216995 -

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Basic information

Entry
Database: PDB / ID: 1bl6
TitleTHE COMPLEX STRUCTURE OF THE MAP KINASE P38/SB216995
ComponentsPROTEIN (MAP KINASE P38)
KeywordsTRANSFERASE / INHIBITORS / MAP KINASE / SERINE/ THREONINE-PROTEIN KINASE / P38
Function / homology
Function and homology information


stress-activated protein kinase signaling cascade / positive regulation of cyclase activity / Activation of PPARGC1A (PGC-1alpha) by phosphorylation / CD163 mediating an anti-inflammatory response / regulation of synaptic membrane adhesion / stress-induced premature senescence / cell surface receptor protein serine/threonine kinase signaling pathway / 3'-UTR-mediated mRNA stabilization / KSRP (KHSRP) binds and destabilizes mRNA / cartilage condensation ...stress-activated protein kinase signaling cascade / positive regulation of cyclase activity / Activation of PPARGC1A (PGC-1alpha) by phosphorylation / CD163 mediating an anti-inflammatory response / regulation of synaptic membrane adhesion / stress-induced premature senescence / cell surface receptor protein serine/threonine kinase signaling pathway / 3'-UTR-mediated mRNA stabilization / KSRP (KHSRP) binds and destabilizes mRNA / cartilage condensation / positive regulation of myoblast fusion / cellular response to UV-B / Platelet sensitization by LDL / mitogen-activated protein kinase p38 binding / positive regulation of muscle cell differentiation / positive regulation of myotube differentiation / NFAT protein binding / Myogenesis / D-glucose import / regulation of cytokine production involved in inflammatory response / Activation of the AP-1 family of transcription factors / ERK/MAPK targets / p38MAPK cascade / Regulation of MITF-M-dependent genes involved in pigmentation / fatty acid oxidation / MAP kinase kinase activity / cellular response to lipoteichoic acid / response to muramyl dipeptide / response to dietary excess / MAP kinase activity / RHO GTPases Activate NADPH Oxidases / regulation of ossification / cellular response to vascular endothelial growth factor stimulus / signal transduction in response to DNA damage / mitogen-activated protein kinase / negative regulation of hippo signaling / positive regulation of myoblast differentiation / chondrocyte differentiation / vascular endothelial growth factor receptor signaling pathway / positive regulation of cardiac muscle cell proliferation / lipopolysaccharide-mediated signaling pathway / stress-activated MAPK cascade / skeletal muscle tissue development / p38MAPK events / striated muscle cell differentiation / response to muscle stretch / positive regulation of interleukin-12 production / positive regulation of brown fat cell differentiation / positive regulation of erythrocyte differentiation / osteoclast differentiation / DNA damage checkpoint signaling / activated TAK1 mediates p38 MAPK activation / positive regulation of D-glucose import / stem cell differentiation / cellular response to ionizing radiation / negative regulation of inflammatory response to antigenic stimulus / NOD1/2 Signaling Pathway / response to insulin / bone development / negative regulation of canonical Wnt signaling pathway / cell morphogenesis / placenta development / cellular response to virus / platelet activation / VEGFA-VEGFR2 Pathway / spindle pole / positive regulation of protein import into nucleus / osteoblast differentiation / ADP signalling through P2Y purinoceptor 1 / chemotaxis / glucose metabolic process / positive regulation of reactive oxygen species metabolic process / cellular senescence / cellular response to tumor necrosis factor / peptidyl-serine phosphorylation / cellular response to lipopolysaccharide / protein phosphatase binding / angiogenesis / secretory granule lumen / Oxidative Stress Induced Senescence / Regulation of TP53 Activity through Phosphorylation / ficolin-1-rich granule lumen / transcription by RNA polymerase II / cell surface receptor signaling pathway / intracellular signal transduction / nuclear speck / protein serine kinase activity / protein serine/threonine kinase activity / glutamatergic synapse / Neutrophil degranulation / positive regulation of gene expression / regulation of transcription by RNA polymerase II / apoptotic process / enzyme binding / signal transduction / positive regulation of transcription by RNA polymerase II / mitochondrion / extracellular region / nucleoplasm / ATP binding
Similarity search - Function
Mitogen-activated protein kinase 14 / Mitogen-activated protein (MAP) kinase p38-like / Mitogen-activated protein (MAP) kinase, conserved site / MAP kinase signature. / : / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Protein kinase domain ...Mitogen-activated protein kinase 14 / Mitogen-activated protein (MAP) kinase p38-like / Mitogen-activated protein (MAP) kinase, conserved site / MAP kinase signature. / : / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / 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 / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-SB6 / Mitogen-activated protein kinase 14
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsWang, Z. / Canagarajah, B.J. / Boehm, J.C. / Kassis, S. / Cobb, M.H. / Young, P.R. / Abdel-Meguid, S. / Adams, J.L. / Goldsmith, E.J.
Citation
Journal: Structure / Year: 1998
Title: Structural basis of inhibitor selectivity in MAP kinases.
Authors: Wang, Z. / Canagarajah, B.J. / Boehm, J.C. / Kassisa, S. / Cobb, M.H. / Young, P.R. / Abdel-Meguid, S. / Adams, J.L. / Goldsmith, E.J.
#1: Journal: J.Biol.Chem. / Year: 1995
Title: Pro-Inflammatory Cytokines and Environmental Stress Cause P38 Mitogen- Activated Protein Kinase Activation by Dual Phosphorylation on Tyrosine and Threonine
Authors: Raingeaud, J. / Gupta, S. / Rogers, J.S. / Dickens, M. / Han, J. / Ulevitch, R.J. / Davis, R.J.
#2: Journal: Science / Year: 1994
Title: A Map Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells
Authors: Han, J. / Lee, J.D. / Bibbs, L. / Ulevitch, R.J.
#3: Journal: Nature / Year: 1994
Title: A Protein Kinase Involved in the Regulation of Inflammatory Cytokine Biosynthesis
Authors: Lee, J.C. / Laydon, J.T. / Mcdonnell, P.C. / Gallagher, T.F. / Kumar, S. / Green, D. / Mcnulty, D. / Blumenthal, M.J. / Heys, J.R. / Landvatter, S.W. / Strickler, J.E. / Mclaughlin, M.M. / ...Authors: Lee, J.C. / Laydon, J.T. / Mcdonnell, P.C. / Gallagher, T.F. / Kumar, S. / Green, D. / Mcnulty, D. / Blumenthal, M.J. / Heys, J.R. / Landvatter, S.W. / Strickler, J.E. / Mclaughlin, M.M. / Siemens, I.R. / Fisher, S.M. / Livi, G.P. / White, J.R. / Adams, J.L. / Young, P.R.
History
DepositionJul 11, 1998Deposition site: BNL / Processing site: RCSB
Revision 1.0Jul 26, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 27, 2023Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Apr 3, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PROTEIN (MAP KINASE P38)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,6772
Polymers43,3831
Non-polymers2931
Water1,29772
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)45.570, 84.710, 123.540
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein PROTEIN (MAP KINASE P38) / MITOGEN ACTIVATED PROTEIN KINASE


Mass: 43383.352 Da / Num. of mol.: 1 / Mutation: 19 RESIDUES INSERTED AT N-TERMINUS
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Strain: BL21 (DE3) / Plasmid: PET15B / Species (production host): Escherichia coli / Cell line (production host): BL21(DE3) / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q16539
#2: Chemical ChemComp-SB6 / 4-(4-FLUOROPHENYL)-1-CYCLOROPROPYLMETHYL-5-(4-PYRIDYL)-IMIDAZOLE / SB216995 / PYRIDINYLIMIDAZOLE / SB216995 / PYRIDINYLIMIDAZOLE


Mass: 293.338 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H16FN3
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 72 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.92 Å3/Da / Density % sol: 58 %
Crystal growpH: 7.4
Details: THE PROTEIN CRYSTALLIZED IN 18% PEG 8000, 0.2M MG(OAC)2, 0.1M HEPES, PH 7.0. THE PROTEIN CONCENTRATION WAS ~10MG/ML IN A BUFFER OF 50MM NACL, 1MM EDTA, 10MM DTT, 1MM BENZAMIDINE, 1UM ...Details: THE PROTEIN CRYSTALLIZED IN 18% PEG 8000, 0.2M MG(OAC)2, 0.1M HEPES, PH 7.0. THE PROTEIN CONCENTRATION WAS ~10MG/ML IN A BUFFER OF 50MM NACL, 1MM EDTA, 10MM DTT, 1MM BENZAMIDINE, 1UM PEPSTATIN, 10UG/ML LEUPEPTIN, 25MM HEPES, PH 7.4.
Crystal grow
*PLUS
Method: vapor diffusion
Details: Wang, Z., (1997) Proc. Natl. Acad. Sci. USA, 94, 2327.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
110 mg/mlprotein1drop
250 mM1dropNaCl
31 mMEDTA1drop
410 mMdithiothreitol1drop
51 mMbenzamidine1drop
60.001 mMpepstasin1drop
70.01 mMleupeptin1drop
825 mMHEPES1drop
918 %PEG80001reservoir
100.2 M1reservoirMg(OAc)2
110.1 MHEPES1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.54
DetectorType: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jan 7, 1997 / Details: MIRRORS
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2.45→38.2 Å / Num. obs: 18307 / % possible obs: 98.2 % / Observed criterion σ(I): -3 / Redundancy: 18.8 % / Rsym value: 0.054 / Net I/σ(I): 21
Reflection shellResolution: 2.45→2.54 Å / Rmerge(I) obs: 0.324 / Mean I/σ(I) obs: 3.6 / % possible all: 90.1
Reflection
*PLUS
Num. measured all: 344423 / Rmerge(I) obs: 0.054

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Processing

Software
NameVersionClassification
AMoRE(CCP4)phasing
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
CCP4phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: MAP KINASE P38

Resolution: 2.5→20 Å / σ(F): 2
RfactorNum. reflection% reflectionSelection details
Rfree0.251 -10 %RANDOM
Rwork0.185 ---
obs0.185 18098 --
Displacement parametersBiso mean: 45.8 Å2
Refinement stepCycle: LAST / Resolution: 2.5→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2833 0 22 72 2927
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.008
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.365
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d25.54
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d0.677
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2PARAM19.SOLTOPH19.SOL
X-RAY DIFFRACTION3SB2.PARSB2.TOP
Software
*PLUS
Name: X-PLOR / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.5 Å / σ(F): 2 / % reflection Rfree: 10 %
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 45.8 Å2
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg25.54
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg0.677

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