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- SASDGD5: The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) bou... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDGD5 |
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![]() | The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) bound to RRESEI peptide (Paused SEC)
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Function / homology | ![]() LGI-ADAM interactions / P2Y1 nucleotide receptor binding / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function |
Biological species | ![]() ![]() |
![]() | ![]() Title: How the dual PDZ domain from Postsynaptic density protein 95 clusters ion channels and receptors Authors: Rodzli N / Lockhart-Cairns M / Levy C / Chipperfield J / Bird L / Baldock C |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Related structure data | C: citing same article ( |
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Similar structure data |
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External links
Related items in Molecule of the Month |
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-Models
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Sample
![]() | Name: The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) bound to RRESEI peptide (Paused SEC) Specimen concentration: 15 mg/ml |
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Buffer | Name: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM RRESEI / pH: 8.5 / Comment: standard buffer plus 10mM ligand peptide |
Entity #1889 | Name: PDZ1-2 / Type: protein Description: PDZ1-2 fragment of PSD-95/Disks large homolog 4 Formula weight: 20.8 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P78352 Sequence: GPGTEGEMEY EEITLERGNS GLGFSIAGGT DNPHIGDDPS IFITKIIPGG AAAQDGRLRV NDSILFVNEV DVREVTHSAA VEALKEAGSI VRLYVMRRKP PAEKVMEIKL IKGPKGLGFS IAGGVGNQHI PGDNSIYVTK IIEGGAAHKD GRLQIGDKIL AVNSVGLEDV ...Sequence: GPGTEGEMEY EEITLERGNS GLGFSIAGGT DNPHIGDDPS IFITKIIPGG AAAQDGRLRV NDSILFVNEV DVREVTHSAA VEALKEAGSI VRLYVMRRKP PAEKVMEIKL IKGPKGLGFS IAGGVGNQHI PGDNSIYVTK IIEGGAAHKD GRLQIGDKIL AVNSVGLEDV MHEDAVAALK NTYDVVYLKV AKPSNA |
-Experimental information
Beam | Instrument name: Diamond Light Source B21 / City: Didcot / 国: UK ![]() ![]() ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 2M | ||||||||||||||||||||||||||||||
Scan | Measurement date: Jan 26, 2016 / Exposure time: 10 sec. / Number of frames: 69 / Unit: 1/A /
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Distance distribution function P(R) |
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Result | Comments: Scattering data are fitted using the ATSAS OLIGOMER program using a suite of models. The ATSAS program FFMAKER was used to generate form factors for each model in the suite. Each model is ...Comments: Scattering data are fitted using the ATSAS OLIGOMER program using a suite of models. The ATSAS program FFMAKER was used to generate form factors for each model in the suite. Each model is assigned a volume fraction to fit the observed scattering profile. 3 monomer models are included, the first is a compact conformation of PDZ1-2 similar to PDB entries 6spv/6spz; the other two are domain models obtained from a representative run of the ATSAS EOM program with data projected to infinite dilution. Multimeric models are drawn from a "clustering Spacegroup", unit cell 14.8nm symmetry I2(1)3, and consist of identical copies of an extended conformation of PDZ1-2 (similar to PDB entry 3zrt) assembled by symmetry operations. In the order of deposition: Model number; Stoichiometry; MW (kDa); source; Volume fraction. 1; 1; 21; Crystal Structure; 0.381. 2; 1; 21; EOM; 0.091. 3; 1; 21; EOM; 0.470. 4; 2; 42; clustering Spacegroup; 0.042. 5; 4; 84; clustering Spacegroup; 0.015. 6; 8; 168; clustering Spacegroup; 0.000. 7; 12, 252; clustering Spacegroup; 0.001. 8; 16, 336, clustering Spacegroup; 0.000. 9; 20, 420, clustering Spacegroup; 0.000. 10; 24, 504, clustering Spacegroup; 0.001.
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