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Yorodumi- PDB-1sps: BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1sps | ||||||
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Title | BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND PEPTIDE-FREE FORMS | ||||||
Components |
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Keywords | TRANSFERASE(PHOSPHOTRANSFERASE) | ||||||
Function / homology | Function and homology information host cell membrane / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / phosphorylation / ATP binding / membrane Similarity search - Function | ||||||
Biological species | Rous sarcoma virus Hamster polyomavirus | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.7 Å | ||||||
Authors | Waksman, G. / Kuriyan, J. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1993 Title: Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Authors: Waksman, G. / Shoelson, S.E. / Pant, N. / Cowburn, D. / Kuriyan, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1sps.cif.gz | 89.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1sps.ent.gz | 74.2 KB | Display | PDB format |
PDBx/mmJSON format | 1sps.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sp/1sps ftp://data.pdbj.org/pub/pdb/validation_reports/sp/1sps | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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Atom site foot note | 1: ILE D 7 - PRO D 8 OMEGA =210.98 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
-Components
#1: Protein | Mass: 11970.480 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rous sarcoma virus / Genus: Alpharetrovirus / References: UniProt: P00524 #2: Protein/peptide | Mass: 1473.515 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Hamster polyomavirus / Genus: PolyomavirusPolyomaviridae / References: UniProt: P03079 #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.98 Å3/Da / Density % sol: 58.78 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8 / Method: other | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 20 Å / Num. obs: 11714 / % possible obs: 89.1 % / Num. measured all: 19885 / Rmerge(I) obs: 0.067 |
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-Processing
Software |
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Refinement | Rfactor Rwork: 0.18 / Rfactor obs: 0.18 / Highest resolution: 2.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.7 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å / Num. reflection obs: 11420 / σ(I): 2 / Rfactor obs: 0.18 / Rfactor Rwork: 0.18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.2 |