1DNY

SOLUTION STRUCTURE OF PCP, A PROTOTYPE FOR THE PEPTIDYL CARRIER DOMAINS OF MODULAR PEPTIDE SYNTHETASES


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 21 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases.

Weber, T.Baumgartner, R.Renner, C.Marahiel, M.A.Holak, T.A.

(2000) Structure 8: 407-418

  • DOI: https://doi.org/10.1016/s0969-2126(00)00120-9
  • Primary Citation of Related Structures:  
    1DNY

  • PubMed Abstract: 

    Nonribosomal peptide synthetases (NRPSs) are large modular enzymes responsible for the synthesis of a variety of microbial bioactive peptides. They consist of modules that each recognise and incorporate one specific amino acid into the peptide product. A module comprises several domains, which carry out the individual reaction steps. After activation by the adenylation domain, the amino acid substrate is covalently tethered to a 4'-phosphopantetheinyl cofactor of a peptidyl carrier domain (PCP) that passes the substrate to the reaction centres of the consecutive domains.


  • Organizational Affiliation

    Biochemie/Fachbereich Chemie, Philipps-Universität, Marburg, 35032, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NON-RIBOSOMAL PEPTIDE SYNTHETASE PEPTIDYL CARRIER PROTEIN91Brevibacillus brevisMutation(s): 0 
Gene Names: TYCC
UniProt
Find proteins for O30409 (Brevibacillus parabrevis)
Explore O30409 
Go to UniProtKB:  O30409
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO30409
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 21 
  • 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: 2000-05-17
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Database references, Derived calculations
  • Version 1.4: 2022-12-21
    Changes: Database references