1NCS

NMR STUDY OF SWI5 ZINC FINGER DOMAIN 1

Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 46 

wwPDB Validation   3D Report Full Report


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


Literature

The solution structure of the first zinc finger domain of SWI5: a novel structural extension to a common fold.

Dutnall, R.N., Neuhaus, D., Rhodes, D.

(1996) Structure 4: 599-611

  • DOI: https://doi.org/10.1016/s0969-2126(96)00064-0
  • Primary Citation of Related Structures:  
    1NCS

  • PubMed Abstract: 

    The 2Cys-2His (C2-H2) zinc finger is a protein domain commonly used for sequence-specific DNA recognition. The zinc fingers of the yeast transcription factors SWI5 and ACE2 share strong sequence homology, which extends into a region N-terminal to the first finger, suggesting that the DNA-binding domains of these two proteins include additional structural elements.

    • Organizational Affiliation: 

    MRC Laboratory of Molecular Biology, Cambridge, UK.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
TRANSCRIPTIONAL FACTOR SWI547Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: T7
UniProt
Find proteins for P08153 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P08153 
Go to UniProtKB:  P08153
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP08153
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN
Download Ideal Coordinates CCD File 
B [auth A]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 46 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-06-10
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-23
    Changes: Database references, Derived calculations, Other