[English] 日本語
Yorodumi- PDB-1quu: CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1quu | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ | ||||||
Components | HUMAN SKELETAL MUSCLE ALPHA-ACTININ 2 | ||||||
Keywords | CONTRACTILE PROTEIN / TRIPLE-HELIX COILED COIL | ||||||
Function / homology | Function and homology information 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 / negative regulation of protein localization to cell surface / LIM domain binding / postsynaptic actin cytoskeleton ...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 / negative regulation of protein localization to cell surface / LIM domain binding / postsynaptic actin cytoskeleton / positive regulation of cation channel activity / 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 / Nephrin family interactions / cardiac muscle cell development / structural constituent of muscle / sarcomere organization / cortical actin cytoskeleton / 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 / phosphatidylinositol-4,5-bisphosphate binding / titin binding / cytoskeletal protein binding / Ras activation upon Ca2+ influx through NMDA receptor / platelet alpha granule lumen / regulation of membrane potential / nuclear receptor coactivator activity / filopodium / cell projection / protein localization to plasma membrane / 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 | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.5 Å | ||||||
Authors | Djinovic-Carugo, K. / Young, P. / Gautel, M. / Saraste, M. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1999 Title: Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Authors: Djinovic-Carugo, K. / Young, P. / Gautel, M. / Saraste, M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1quu.cif.gz | 66.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1quu.ent.gz | 49.7 KB | Display | PDB format |
PDBx/mmJSON format | 1quu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1quu_validation.pdf.gz | 364.8 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1quu_full_validation.pdf.gz | 376.9 KB | Display | |
Data in XML | 1quu_validation.xml.gz | 7.9 KB | Display | |
Data in CIF | 1quu_validation.cif.gz | 11.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qu/1quu ftp://data.pdbj.org/pub/pdb/validation_reports/qu/1quu | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 29283.828 Da / Num. of mol.: 1 Fragment: SPECTRIN-LIKE REPEATS 2 AND 3 - AMINO ACIDS 391 TO 637 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Tissue: SKELETAL MUSCLE / Plasmid: PET 8C / Production host: Escherichia coli (E. coli) / References: UniProt: P35609 |
---|---|
#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.47 Å3/Da / Density % sol: 64.58 % | |||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 26% PEG 400 (FLUKA), 100 MM MGSO4, 100 MM HEPES OR TRIS-HCL, pH 7.5, VAPOR DIFFUSION, HANGING DROP | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.4 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.947 |
Detector | Type: OFF-LINE SCANNER / Detector: IMAGE PLATE / Date: Feb 10, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.947 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→25 Å / Num. all: 21275 / Num. obs: 21275 / % possible obs: 94.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.1 % / Biso Wilson estimate: 48.6 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 2.2→2.24 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.339 / % possible all: 89.8 |
Reflection | *PLUS |
Reflection shell | *PLUS % possible obs: 89.8 % |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.5→25 Å / σ(F): 2 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→25 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 25 Å / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 57.2 Å2 |