2KB9

Human Jagged-1, exon 6


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Exon 6 of human JAG1 encodes a conserved structural unit

Pintar, A.Guarnaccia, C.Dhir, S.Pongor, S.

(2009) BMC Struct Biol 9: 43-43

  • DOI: https://doi.org/10.1186/1472-6807-9-43
  • Primary Citation of Related Structures:  
    2KB9

  • PubMed Abstract: 

    Notch signaling drives developmental processes in all metazoans. The receptor binding region of the human Notch ligand Jagged-1 is made of a DSL (Delta/Serrate/Lag-2) domain and two atypical epidermal growth factor (EGF) repeats encoded by two exons, exon 5 and 6, which are out of phase with respect to the EGF domain boundaries.


  • Organizational Affiliation

    International Centre for Genetic Engineering and Biotechnology, Protein Structure and Bioinformatics Group, AREA Science Park, Padriciano 99, Trieste, Italy. pintar@icgeb.org


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Jagged-144N/AMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P78504 (Homo sapiens)
Explore P78504 
Go to UniProtKB:  P78504
PHAROS:  P78504
GTEx:  ENSG00000101384 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP78504
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-07-28
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2022-03-16
    Changes: Data collection, Database references, Derived calculations