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- PDB-1nyg: NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1nyg | ||||||
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Title | NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE, FAMILY OF 20 STRUCTURES | ||||||
![]() | FYN | ||||||
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Function / homology | ![]() response to singlet oxygen / Reelin signalling pathway / negative regulation of hydrogen peroxide biosynthetic process / perinuclear endoplasmic reticulum / NTRK2 activates RAC1 / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Morton, C.J. / Pugh, D.J.R. / Campbell, I.D. | ||||||
![]() | ![]() Title: Solution structure and peptide binding of the SH3 domain from human Fyn. Authors: Morton, C.J. / Pugh, D.J. / Brown, E.L. / Kahmann, J.D. / Renzoni, D.A. / Campbell, I.D. #1: ![]() Title: Crystal Structure of the SH3 Domain in Human Fyn; Comparison of the Three-Dimensional Structures of SH3 Domains in Tyrosine Kinases and Spectrin Authors: Noble, M.E. / Musacchio, A. / Saraste, M. / Courtneidge, S.A. / Wierenga, R.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 354.8 KB | Display | ![]() |
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PDB format | ![]() | 295 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 7554.108 Da / Num. of mol.: 1 / Fragment: SH3 DOMAIN, RESIDUES 82 - 148 / Mutation: INS(GS-T82) Source method: isolated from a genetically manipulated source Details: N-TERMINAL GS FROM EXPRESSION SYSTEM / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow![]() | *PLUS Method: other / Details: NMR |
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Processing
Software |
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NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 20 |