2A0T

NMR structure of the FHA1 domain of Rad53 in complex with a biological relevant phosphopeptide derived from Madt1

Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with acceptable covalent geometry, structures with the least restraint violations, structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

FHA Domain-Ligand Interactions: Importance of Integrating Chemical and Biological Approaches

Mahajan, A., Yuan, C., Pike, B.L., Heierhorst, J., Chang, C.-F., Tsai, M.-D.

(2005) J Am Chem Soc 127: 14572-14573

  • DOI: https://doi.org/10.1021/ja054538m
  • Primary Citation of Related Structures:  
    2A0T

  • PubMed Abstract: 

    Combinatorial library screens based on binding affinity may preferentially select ligands with ability for ionic interactions and miss the biologically relevant ligands that bind more weakly with predominantly hydrophobic interactions.

    • Organizational Affiliation: 

    Biophysics Program, The Ohio State University, Columbus, Ohio 43210, USA.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine/threonine-protein kinase RAD53151Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: SPK1 or Rad53
EC: 2.7.1.37
UniProt
Find proteins for P22216 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P22216 
Go to UniProtKB:  P22216
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP22216
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Hypothetical 73.8 kDa protein in SAS3-SEC17 intergenic region, residues 301-31010N/AMutation(s): 1 
UniProt
Find proteins for P34217 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P34217 
Go to UniProtKB:  P34217
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP34217
Sequence Annotations
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  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
TPO
Query on TPO
B
L-PEPTIDE LINKINGC4 H10 N O6 PTHR
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with acceptable covalent geometry, structures with the least restraint violations, structures with the lowest energy 

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-11-08
    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: 2022-03-09
    Changes: Data collection, Database references, Derived calculations