2DDE

Structure of cinnamycin complexed with lysophosphatidylethanolamine

Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history. 


Literature

Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1.

Hosoda, K., Ohya, M., Kohno, T., Maeda, T., Endo, S., Wakamatsu, K.

(1996) J Biochem 119: 226-230

  • DOI: https://doi.org/10.1093/oxfordjournals.jbchem.a021226

  • PubMed Abstract: 

    The three-dimensional structure of a complex of cinnamycin, a 19-amino acid residue immunopotentiator peptide, and lysophosphatidylethanolamine was determined by 1H-NMR. The complex was cylindrical in shape, 11 A in diameter and 26 A in length, excluding the acyl chain of the phospholipid. The peptide had a hydrophobic pocket surrounded by residues Phe-7 through Ala(S)-14 to bind to the head group of the ligand. Fitting of the head group to the hydrophobic pocket was so good that other than a glycerophosphoethanolamine head group would be unable to fit the pocket. The goodness of the fitting is compatible with the strict specificity of ligand binding of the peptide.

    • Organizational Affiliation: 

    Department of Biochemical Sciences, Gunma University.


Macromolecules

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
LANTIBIOTIC CINNAMYCIN19Streptomyces griseoverticillatusMutation(s): 0 
UniProt
Find proteins for P29827 (Streptomyces griseoverticillatus)
Explore P29827 
Go to UniProtKB:  P29827
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29827
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
LSP
Query on LSP
Download Ideal Coordinates CCD File 
B [auth A](7S)-4,7-DIHYDROXY-10-OXO-3,5,9-TRIOXA-4-PHOSPHAUNDECAN-1-AMINIUM 4-OXIDE
C7 H17 N O7 P
CWRILEGKIAOYKP-ZETCQYMHSA-O
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
BH2
Query on BH2
A
L-PEPTIDE LINKINGC4 H7 N O5ASP
Biologically Interesting Molecules (External Reference) 1 Unique
Entity ID: 1
IDChains NameType/Class2D Diagram3D Interactions
PRD_000195
Query on PRD_000195
A
CinnamycinPolypeptide / Lantibiotic
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-02-21
    Type: Initial release
  • Version 1.1: 2011-06-14
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2011-07-27
    Changes: Atomic model, Database references, Derived calculations, Non-polymer description, Structure summary
  • Version 1.4: 2012-12-12
    Changes: Other
  • Version 1.5: 2019-11-06
    Changes: Data collection, Database references, Derived calculations
  • Version 2.0: 2023-11-15
    Changes: Atomic model, Data collection, Database references, Derived calculations