+Open data
-Basic information
Entry | Database: PDB / ID: 7rm8 | |||||||||||||||||||||||||||
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Title | Solution NMR structure of PDLIM7 PDZ bound to SNX17 peptide | |||||||||||||||||||||||||||
Components | Isoform 4 of PDZ and LIM domain protein 7,Sorting nexin-17 fusion | |||||||||||||||||||||||||||
Keywords | STRUCTURAL PROTEIN | |||||||||||||||||||||||||||
Function / homology | Function and homology information muscle structure development / cardiac septum development / muscle alpha-actinin binding / coronary vasculature development / endocytic recycling / aorta development / endosomal transport / low-density lipoprotein particle receptor binding / filamentous actin / regulation of endocytosis ...muscle structure development / cardiac septum development / muscle alpha-actinin binding / coronary vasculature development / endocytic recycling / aorta development / endosomal transport / low-density lipoprotein particle receptor binding / filamentous actin / regulation of endocytosis / RET signaling / cholesterol catabolic process / stress fiber / ruffle / phosphatidylinositol binding / ossification / receptor-mediated endocytosis / kidney development / adherens junction / intracellular protein transport / Z disc / actin cytoskeleton / heart development / actin binding / cytoplasmic vesicle / actin cytoskeleton organization / early endosome / cell differentiation / endosome membrane / endosome / intracellular membrane-bounded organelle / focal adhesion / signaling receptor binding / Golgi apparatus / signal transduction / protein-containing complex / nucleoplasm / membrane / metal ion binding / cytosol Similarity search - Function | |||||||||||||||||||||||||||
Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||
Method | SOLUTION NMR / torsion angle dynamics | |||||||||||||||||||||||||||
Authors | Healy, M.D. / Collins, B.M. / Mobli, M. | |||||||||||||||||||||||||||
Funding support | Australia, United Kingdom, 8items
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Citation | Journal: Structure / Year: 2022 Title: Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins. Authors: Healy, M.D. / Sacharz, J. / McNally, K.E. / McConville, C. / Tillu, V.A. / Hall, R.J. / Chilton, M. / Cullen, P.J. / Mobli, M. / Ghai, R. / Stroud, D.A. / Collins, B.M. | |||||||||||||||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7rm8.cif.gz | 695.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7rm8.ent.gz | 591.2 KB | Display | PDB format |
PDBx/mmJSON format | 7rm8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7rm8_validation.pdf.gz | 402.2 KB | Display | wwPDB validaton report |
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Full document | 7rm8_full_validation.pdf.gz | 532.4 KB | Display | |
Data in XML | 7rm8_validation.xml.gz | 33.9 KB | Display | |
Data in CIF | 7rm8_validation.cif.gz | 54.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rm/7rm8 ftp://data.pdbj.org/pub/pdb/validation_reports/rm/7rm8 | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homologyF&H Search |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11317.567 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PDLIM7, ENIGMA, SNX17, KIAA0064 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9NR12, UniProt: Q15036 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution Contents: 1 mM [U-13C; U-15N] PDLIM7_SNX17_Fusion, 95% H2O/5% D2O Details: Protein was gel filtered in a buffer containing 75 mM NaCl, 20 mM Bis-Tris (pH 5.8), 4 mM DTT. Label: PDLIM7_SNX17_Fusion / Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Details: Protein was gel filtered in a buffer containing 75 mM NaCl, 20 mM Bis-Tris (pH 5.8), 4 mM DTT. Ionic strength: 75 mM NaCl mM / Label: Condition 1 / pH: 5.8 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 20 |