1X0N

NMR structure of growth factor receptor binding protein SH2 domain complexed with the inhibitor


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

NMR structure of growth factor receptor binding protein SH2 domain complexed with the inhibitor

Ogura, K.Shiga, T.Yuzawa, S.Yokochi, M.Burke, T.R.Inagaki, F.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Growth factor receptor-bound protein 2104Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P62993 (Homo sapiens)
Explore P62993 
Go to UniProtKB:  P62993
PHAROS:  P62993
GTEx:  ENSG00000177885 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP62993
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
DTF
Query on DTF

Download Ideal Coordinates CCD File 
B [auth A]4-[(10S,14S,18S)-18-(2-AMINO-2-OXOETHYL)-14-(1-NAPHTHYLMETHYL)-8,17,20-TRIOXO-7,16,19-TRIAZASPIRO[5.14]ICOS-11-EN-10-YL]BENZYLPHOSPHONIC ACID
C37 H45 N4 O7 P
RHYFMOCFCFUTNH-GZNVFMSSSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
DTF PDBBind:  1X0N IC50: 20 (nM) from 1 assay(s)
BindingDB:  1X0N IC50: min: 20, max: 26 (nM) from 2 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-04-19
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Data collection, Database references, Derived calculations