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- PDB-1ydt: STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUN... -
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Basic information
Entry | Database: PDB / ID: 1ydt | ||||||
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Title | STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H89 PROTEIN KINASE INHIBITOR N-[2-(4-BROMOCINNAMYLAMINO)ETHYL]-5-ISOQUINOLINE | ||||||
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![]() | COMPLEX (PHOSPHOTRANSFERASE/INHIBITOR) / COMPLEX (PHOSPHOTRANSFERASE-INHIBITOR) / TRANSFERASE / CAMP / PHOSPHORYLATION / ISOQUINOLINE SULFONAMIDE / SERINE/THREONINE-PROTEIN KINASE / ATP-BINDING / COMPLEX (PHOSPHOTRANSFERASE-INHIBITOR) complex | ||||||
Function / homology | ![]() CD209 (DC-SIGN) signaling / HDL assembly / Regulation of insulin secretion / Rap1 signalling / Ion homeostasis / PKA activation in glucagon signalling / DARPP-32 events / CREB1 phosphorylation through the activation of Adenylate Cyclase / GPER1 signaling / Factors involved in megakaryocyte development and platelet production ...CD209 (DC-SIGN) signaling / HDL assembly / Regulation of insulin secretion / Rap1 signalling / Ion homeostasis / PKA activation in glucagon signalling / DARPP-32 events / CREB1 phosphorylation through the activation of Adenylate Cyclase / GPER1 signaling / Factors involved in megakaryocyte development and platelet production / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / RET signaling / Interleukin-3, Interleukin-5 and GM-CSF signaling / Recruitment of NuMA to mitotic centrosomes / VEGFA-VEGFR2 Pathway / PKA activation / negative regulation of cAMP-dependent protein kinase activity / GLI3 is processed to GLI3R by the proteasome / MAPK6/MAPK4 signaling / Regulation of PLK1 Activity at G2/M Transition / Hedgehog 'off' state / cAMP-dependent protein kinase inhibitor activity / cAMP-dependent protein kinase / cAMP-dependent protein kinase activity / cAMP-dependent protein kinase complex / AMP-activated protein kinase activity / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / negative regulation of protein import into nucleus / Vasopressin regulates renal water homeostasis via Aquaporins / Mitochondrial protein degradation / protein kinase A regulatory subunit binding / protein kinase A catalytic subunit binding / mesoderm formation / sperm flagellum / negative regulation of TORC1 signaling / regulation of G2/M transition of mitotic cell cycle / protein kinase A signaling / acrosomal vesicle / neuromuscular junction / cellular response to heat / peptidyl-serine phosphorylation / protein kinase activity / protein domain specific binding / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / mitochondrion / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Engh, R.A. / Girod, A. / Kinzel, V. / Huber, R. / Bossemeyer, D. | ||||||
![]() | ![]() Title: Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity. Authors: Engh, R.A. / Girod, A. / Kinzel, V. / Huber, R. / Bossemeyer, D. #1: ![]() Title: Phosphotransferase and Substrate Binding Mechanism of the Camp-Dependent Protein Kinase Catalytic Subunit from Porcine Heart as Deduced from the 2.0 A Structure of the Complex with Mn2+ ...Title: Phosphotransferase and Substrate Binding Mechanism of the Camp-Dependent Protein Kinase Catalytic Subunit from Porcine Heart as Deduced from the 2.0 A Structure of the Complex with Mn2+ Adenylyl Imidodiphosphate and Inhibitor Peptide Pki(5-24) Authors: Bossemeyer, D. / Engh, R.A. / Kinzel, V. / Ponstingl, H. / Huber, R. #2: ![]() Title: Cloning of the C Alpha Catalytic Subunit of the Bovine Camp-Dependent Protein Kinase Authors: Wiemann, S. / Kinzel, V. / Pyerin, W. #3: ![]() Title: Inhibition of Forskolin-Induced Neurite Outgrowth and Protein Phosphorylation by a Newly Synthesized Selective Inhibitor of Cyclic AMP-Dependent Protein Kinase, N-[2-(Para-Bromocinnamylamino) ...Title: Inhibition of Forskolin-Induced Neurite Outgrowth and Protein Phosphorylation by a Newly Synthesized Selective Inhibitor of Cyclic AMP-Dependent Protein Kinase, N-[2-(Para-Bromocinnamylamino) Ethyl]-5-Isoquinolinesulfonamide (H-89), of Pc12D Pheochromocytoma Cells Authors: Chijiwa, T. / Mishima, A. / Hagiwara, M. / Sano, M. / Hayashi, K. / Inoue, T. / Naito, K. / Toshioka, T. / Hidaka, H. #4: ![]() Title: Isoquinolinesulfonamides, Novel and Potent Inhibitors of Cyclic Nucleotide Dependent Protein Kinase and Protein Kinase C Authors: Hidaka, H. / Inagaki, M. / Kawamoto, S. / Sasaki, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 40681.363 Da / Num. of mol.: 1 / Fragment: CATALYTIC SUBUNIT Source method: isolated from a genetically manipulated source Details: ALPHA ISOENZYME / Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 2226.411 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P04541, UniProt: P63249*PLUS |
#3: Chemical | ChemComp-IQB / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.31 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.5 Details: 15 % METHANOL, 70 MILLIMOLAR SODIUM SULFATE, 20 MILLIMOLAR MES-BIS-TRIS PH 6.5, 279K USING HANGING DROP DIFFUSION., vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 5 ℃ / Method: vapor diffusion, hanging drop / PH range low: 6.6 / PH range high: 6.3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 12157 / % possible obs: 62 % |
Reflection | *PLUS Highest resolution: 2.3 Å / Rmerge(I) obs: 0.058 |
Reflection shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.39 Å / % possible obs: 26 % |
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Processing
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Refinement | Resolution: 2.3→6 Å / Rfactor Rwork: 0.194 / Rfactor obs: 0.194 / σ(F): 3 Details: ONLY THE WATER MOLECULES IN THE VICINITY OF THE BOUND H-89 INHIBITOR MOLECULE HAVE BEEN MODELED. | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Software | *PLUS Name: ![]() | ||||||||||||
Refinement | *PLUS Num. reflection obs: 12157 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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