2EDX

Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations, target function 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F

Sato, M.Koshiba, S.Inoue, M.Kigawa, T.Yokoyama, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein tyrosine phosphatase, receptor type, F134Homo sapiensMutation(s): 0 
Gene Names: PTPRF
EC: 3.1.3.48
UniProt & NIH Common Fund Data Resources
Find proteins for P10586 (Homo sapiens)
Explore P10586 
Go to UniProtKB:  P10586
PHAROS:  P10586
GTEx:  ENSG00000142949 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP10586
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the least restraint violations, target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-08-21
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2022-03-09
    Changes: Data collection, Database references, Derived calculations
  • Version 1.3: 2024-05-29
    Changes: Data collection