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Open data
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Basic information
Entry | Database: PDB / ID: 1h8b | ||||||
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Title | EF-hands 3,4 from alpha-actinin / Z-repeat 7 from titin | ||||||
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![]() | STRUCTURAL PROTEIN / Z-DISK STRUCTURAL COMPLEX | ||||||
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 / telethonin binding / postsynaptic actin cytoskeleton / positive regulation of cation channel activity ...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 / telethonin binding / 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 / intracellular non-membrane-bounded organelle / 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 | SOLUTION NMR / TORSION ANGLE DYNAMICS, CARTESIAN DYANMICS | ||||||
![]() | Atkinson, R.A. / Joseph, C. / Kelly, G. / Muskett, F.W. / Frenkiel, T.A. / Nietlispach, D. / Pastore, A. | ||||||
![]() | ![]() Title: Ca2+-Independent Binding of an EF-Hand Domain to a Novel Motif in the Alpha-Actinin-Titin Complex Authors: Atkinson, R.A. / Joseph, C. / Kelly, G. / Muskett, F.W. / Frenkiel, T.A. / Nietlispach, D. / Pastore, A. #1: Journal: Biochemistry / Year: 2000 Title: The Binding of Alpha-Actinin to Titin: Implications for Z-Disk Assembly Authors: Atkinson, R.A. / Joseph, C. / Piaz, F.D. / Birolo, L. / Stier, G. / Pucci, P. / Pastore, A. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 845.8 KB | Display | ![]() |
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PDB format | ![]() | 713.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 355.5 KB | Display | ![]() |
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Full document | ![]() | 779.7 KB | Display | |
Data in XML | ![]() | 58.5 KB | Display | |
Data in CIF | ![]() | 90.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 8077.011 Da / Num. of mol.: 1 / Fragment: EF-HANDS 3&4 RESIDUE 822-894 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 5667.321 Da / Num. of mol.: 1 / Fragment: Z-REPEAT 7 RESIDUES 648-698 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
Compound details | CHAIN A ENGINEERED MUTATION THR822MET, MODIFIED FOR EXPRESSION F-ACTIN CROSS-LINKING PROTEIN IS ...CHAIN A ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: SEE PUBLICATION |
NMR details | Text: THE STRUCTURE OF THE COMPLEX WAS DETERMINED USING CONSTRAINTS FROM 15N-EDITED NOESY, 13C-EDITED NOESY AND F1-FILTERED/F3-EDITED NOESY SPECTRA, RECORDED ON 13C, 15N-LABELLED SAMPLES IN WHICH ...Text: THE STRUCTURE OF THE COMPLEX WAS DETERMINED USING CONSTRAINTS FROM 15N-EDITED NOESY, 13C-EDITED NOESY AND F1-FILTERED/F3-EDITED NOESY SPECTRA, RECORDED ON 13C, 15N-LABELLED SAMPLES IN WHICH ONLY ONE OF THE TWO COMPONENTS WAS LABELLED |
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Sample preparation
Details | Contents: 0.7 MM COMPLEX |
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Sample conditions | Ionic strength: 20 mM / pH: 6.6 / Pressure: 1 atm / Temperature: 300 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: TORSION ANGLE DYNAMICS, CARTESIAN DYANMICS / Software ordinal: 1 Details: REFINEMENT DETAILS MAY BE FOUND IN THE JRNL CITATION ABOVE THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF ALPHA-ACTININ EF34 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. ...Details: REFINEMENT DETAILS MAY BE FOUND IN THE JRNL CITATION ABOVE THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF ALPHA-ACTININ EF34 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE CONSTRAINTS FOR THESE TWO RESIDUES WHICH ARE OMITTED FROM THE STRUCTURE CALCULATION. THE FIRST RESIDUE OF THE NATURAL SEQUENCE OF TITIN ZR7 IS REPLACED BY A MET. THIS IS PRECEDED BY THE DIPEPTIDE GLY-ALA. THERE ARE NO DISTANCE CONSTRAINTS FOR THE N-TERMINAL 8 RESIDUES AND THE C-TERMINAL 22 RESIDUES WHICH ARE OMITTED FROM THE STRUCTURE CALCULATION. | ||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGIES / Conformers calculated total number: 50 / Conformers submitted total number: 30 |