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Open data
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Basic information
Entry | Database: PDB / ID: 8p35 | ||||||||||||
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Title | Mutant human titin immunoglobulin-like 21 domain - C3575S | ||||||||||||
![]() | Titin | ||||||||||||
![]() | STRUCTURAL PROTEIN / Titin / Muscle / Immunoglobulin-like | ||||||||||||
Function / homology | ![]() sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / cardiac muscle tissue morphogenesis / regulation of catalytic activity / cardiac muscle hypertrophy ...sarcomerogenesis / structural molecule activity conferring elasticity / telethonin binding / skeletal muscle myosin thick filament assembly / cardiac myofibril assembly / muscle alpha-actinin binding / detection of muscle stretch / cardiac muscle tissue morphogenesis / regulation of catalytic activity / cardiac muscle hypertrophy / mitotic chromosome condensation / Striated Muscle Contraction / actinin binding / M band / I band / cardiac muscle cell development / regulation of protein kinase activity / structural constituent of muscle / sarcomere organization / skeletal muscle thin filament assembly / striated muscle thin filament / striated muscle contraction / cardiac muscle contraction / protein kinase A signaling / condensed nuclear chromosome / muscle contraction / positive regulation of protein secretion / Z disc / response to calcium ion / : / actin filament binding / Platelet degranulation / protein tyrosine kinase activity / protease binding / non-specific serine/threonine protein kinase / calmodulin binding / phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / calcium ion binding / positive regulation of gene expression / protein kinase binding / enzyme binding / extracellular exosome / extracellular region / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Martinez-Martin, I. / Crousilles, A. / Mortensen, S.A. / Alegre-Cebollada, J. / Wilmanns, M. | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Titin domains with reduced core hydrophobicity cause dilated cardiomyopathy. Authors: Martinez-Martin, I. / Crousilles, A. / Ochoa, J.P. / Velazquez-Carreras, D. / Mortensen, S.A. / Herrero-Galan, E. / Delgado, J. / Dominguez, F. / Garcia-Pavia, P. / de Sancho, D. / Wilmanns, ...Authors: Martinez-Martin, I. / Crousilles, A. / Ochoa, J.P. / Velazquez-Carreras, D. / Mortensen, S.A. / Herrero-Galan, E. / Delgado, J. / Dominguez, F. / Garcia-Pavia, P. / de Sancho, D. / Wilmanns, M. / Alegre-Cebollada, J. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 275.1 KB | Display | ![]() |
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PDB format | ![]() | 179.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 456.6 KB | Display | ![]() |
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Full document | ![]() | 463.1 KB | Display | |
Data in XML | ![]() | 23.2 KB | Display | |
Data in CIF | ![]() | 33.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8ovuC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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: 10809.206 Da / Num. of mol.: 6 / Mutation: C3575S Source method: isolated from a genetically manipulated source Details: The first N-terminal glycine of the sequence corresponds to a linker used for the cloning strategy and it is followed by the sequence of the mutant human Ig 21 domain. In this mutant the ...Details: The first N-terminal glycine of the sequence corresponds to a linker used for the cloning strategy and it is followed by the sequence of the mutant human Ig 21 domain. In this mutant the native cysteine in position 76 is replaced by a serine. Source: (gene. exp.) ![]() Details (production host): Expression vector containing a HisTag and a thioredoxin tag, both cleavable by TEV protease Production host: ![]() ![]() References: UniProt: Q8WZ42, non-specific serine/threonine protein kinase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.82 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1 M HEPES sodium salt, pH 7.5, 25 %(w/v) PEG 2000 MME |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 5, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→48.21 Å / Num. obs: 35855 / % possible obs: 100 % / Redundancy: 24.5 % / CC1/2: 0.995 / Rmerge(I) obs: 0.08 / Rpim(I) all: 0.024 / Net I/σ(I): 22.6 |
Reflection shell | Resolution: 2.2→2.27 Å / Rmerge(I) obs: 0.4 / Num. unique obs: 3088 / CC1/2: 0.984 / Rpim(I) all: 0.116 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 42.85 Å2 | ||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→48.21 Å
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LS refinement shell | Resolution: 2.2→2.27 Å / Rfactor Rfree: 0.346 / Rfactor Rwork: 0.271 |