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Open data
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Basic information
Entry | Database: PDB / ID: 1hci | ||||||
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Title | CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ | ||||||
![]() | ALPHA-ACTININ 2 | ||||||
![]() | TRIPLE-HELIX COILED COIL / CONTRACTILE PROTEIN / MUSCLE / Z-LINE / ACTIN-BINDING PROTEIN | ||||||
Function / homology | ![]() actin filament uncapping / FATZ binding / titin Z domain binding / phospholipase C-activating angiotensin-activated signaling pathway / positive regulation of endocytic recycling / positive regulation of potassium ion transmembrane transporter activity / negative regulation of potassium ion transmembrane transporter activity / postsynaptic actin cytoskeleton / positive regulation of cation channel activity / negative regulation of protein localization to cell surface ...actin filament uncapping / FATZ binding / titin Z domain binding / phospholipase C-activating angiotensin-activated signaling pathway / positive regulation of endocytic recycling / positive regulation of potassium ion transmembrane transporter activity / negative regulation of potassium ion transmembrane transporter activity / postsynaptic actin cytoskeleton / positive regulation of cation channel activity / negative regulation of protein localization to cell surface / LIM domain binding / microspike assembly / positive regulation of potassium ion transport / muscle cell development / focal adhesion assembly / Striated Muscle Contraction / Assembly and cell surface presentation of NMDA receptors / cardiac muscle cell development / Nephrin family interactions / structural constituent of muscle / cortical actin cytoskeleton / sarcomere organization / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / pseudopodium / negative regulation of potassium ion transport / Long-term potentiation / postsynaptic density, intracellular component / titin binding / cytoskeletal protein binding / phosphatidylinositol-4,5-bisphosphate binding / Ras activation upon Ca2+ influx through NMDA receptor / nuclear receptor coactivator activity / platelet alpha granule lumen / filopodium / cell projection / protein localization to plasma membrane / regulation of membrane potential / actin filament / postsynaptic density membrane / Z disc / actin filament binding / integrin binding / Platelet degranulation / cell junction / actin cytoskeleton organization / RAF/MAP kinase cascade / regulation of apoptotic process / transmembrane transporter binding / dendritic spine / cytoskeleton / cell adhesion / protein domain specific binding / focal adhesion / glutamatergic synapse / calcium ion binding / extracellular exosome / extracellular region / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ylanne, J. / Scheffzek, K. / Young, P. / Saraste, M. | ||||||
![]() | ![]() Title: Crystal Structure of the Alpha-Actinin Rod Reveals an Extensive Torsional Twist Authors: Ylanne, J. / Scheffzek, K. / Young, P. / Saraste, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 202.1 KB | Display | ![]() |
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PDB format | ![]() | 162.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440.2 KB | Display | ![]() |
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Full document | ![]() | 493.1 KB | Display | |
Data in XML | ![]() | 39.3 KB | Display | |
Data in CIF | ![]() | 52.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1quuS S: Starting model for refinement |
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Similar 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: 56211.324 Da / Num. of mol.: 2 Fragment: SPECTRIN-LIKE REPEATS 1,2,3, AND 4 - AMINO ACIDS 274 - 746 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | Sequence details | PDB CONTAINS N-TERM GLY SER SER FROM THE VECTOR | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density % sol: 80.3 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: 0.9 M (NH4)2SO4, 0.1 M TRISHCL PH 8.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 8.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 2, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→82.78 Å / Num. obs: 63392 / % possible obs: 98.7 % / Observed criterion σ(I): 0 / Redundancy: 2.45 % / Biso Wilson estimate: 21.6 Å2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 7.6 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 1.78 % / Rmerge(I) obs: 0.261 / Mean I/σ(I) obs: 2.28 / % possible all: 99 |
Reflection | *PLUS Num. measured all: 155820 |
Reflection shell | *PLUS % possible obs: 99 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1QUU Resolution: 2.8→82.78 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 3989928.9 / Cross valid method: THROUGHOUT / σ(F): 0 Stereochemistry target values: MAXIMUM LIKEHOOD USING AMPLITUDES
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 58.9267 Å2 / ksol: 0.367476 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 71.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→82.78 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.98 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.27 / Rfactor Rwork: 0.27 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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