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Open data
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Basic information
Entry | Database: PDB / ID: 9b3r | |||||||||
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Title | The structure of human cardiac F-actin | |||||||||
![]() | Actin, alpha cardiac muscle 1 | |||||||||
![]() | CONTRACTILE PROTEIN / actin / cardiac / human / sarcomere | |||||||||
Function / homology | ![]() actin-myosin filament sliding / actin filament-based movement / cardiac myofibril assembly / cardiac muscle tissue morphogenesis / actomyosin structure organization / Striated Muscle Contraction / I band / microfilament motor activity / RHOB GTPase cycle / myosin binding ...actin-myosin filament sliding / actin filament-based movement / cardiac myofibril assembly / cardiac muscle tissue morphogenesis / actomyosin structure organization / Striated Muscle Contraction / I band / microfilament motor activity / RHOB GTPase cycle / myosin binding / heart contraction / mesenchyme migration / skeletal muscle thin filament assembly / RHOA GTPase cycle / sarcomere / filopodium / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / lamellipodium / cell body / blood microparticle / hydrolase activity / focal adhesion / glutamatergic synapse / positive regulation of gene expression / negative regulation of apoptotic process / extracellular space / extracellular exosome / ATP binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Doran, M.H. / Sousa, D. / Rynkiewicz, M.J. / Lehman, W. / Cammarato, A. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of human cardiac actin Authors: Doran, M.H. / Rynkiewicz, M.J. / Sousa, D. / Cammarato, A. / Lehman, W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 198.4 KB | Display | ![]() |
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PDB format | ![]() | 160 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 44154MC ![]() 9b3qC M: map data used to model this data 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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Components
#1: Protein | Mass: 42077.910 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P68032, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement #2: Chemical | #3: Chemical | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
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Sample preparation
Component | Name: Human cardiac F-actin / Type: COMPLEX Details: ACTC was expressed in Sf21 insect cells, using recombinant baculoviruses, and purified via gelsolin affinity chromatography Entity ID: #1 / Source: RECOMBINANT |
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Molecular weight | Value: .42 MDa / Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 8 Details: 2 mmolL-1 Tris (pH 8), 0.2 mmolL-1 CaCl2, 0.2 mmolL-1 ATP, 0.5 mmolL-1 b-mercaptoethanol, 0.002% NaN3 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 8000 nm / Nominal defocus min: 600 nm |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
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Helical symmerty | Angular rotation/subunit: -166.48 ° / Axial rise/subunit: 27.93 Å / Axial symmetry: C1 | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 133289 / Symmetry type: HELICAL | ||||||||||||||||||||||||
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