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- PDB-2pdd: THE HIGH RESOLUTION STRUCTURE OF THE PERIPHERAL SUBUNIT-BINDING D... -

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Basic information

Entry
Database: PDB / ID: 2pdd
TitleTHE HIGH RESOLUTION STRUCTURE OF THE PERIPHERAL SUBUNIT-BINDING DOMAIN OF DIHYDROLIPOAMIDE ACETYLTRANSFERASE FROM THE PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX OF BACILLUS STEAROTHERMOPHILUS
ComponentsDIHYDROLIPOAMIDE ACETYLTRANSFERASE
KeywordsOXIDOREDUCTASE / OXIDO-REDUCTASE(ACYLTRANSFERASE)
Function / homology
Function and homology information


dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / cytoplasm
Similarity search - Function
E3-binding domain / Dihydrolipoamide Transferase / : / Peripheral subunit-binding domain / e3 binding domain / Peripheral subunit-binding (PSBD) domain profile. / E3-binding domain superfamily / 2-oxo acid dehydrogenase, lipoyl-binding site / 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. / 2-oxoacid dehydrogenase acyltransferase, catalytic domain ...E3-binding domain / Dihydrolipoamide Transferase / : / Peripheral subunit-binding domain / e3 binding domain / Peripheral subunit-binding (PSBD) domain profile. / E3-binding domain superfamily / 2-oxo acid dehydrogenase, lipoyl-binding site / 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. / 2-oxoacid dehydrogenase acyltransferase, catalytic domain / 2-oxoacid dehydrogenases acyltransferase (catalytic domain) / Biotin-requiring enzyme / Biotinyl/lipoyl domain profile. / Biotin/lipoyl attachment / Single hybrid motif / Chloramphenicol acetyltransferase-like domain superfamily / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Similarity search - Component
MethodSOLUTION NMR
AuthorsKalia, Y.N. / Brocklehurst, S.M. / Hipps, D.S. / Appella, E. / Sakaguchi, K. / Perham, R.N.
CitationJournal: J.Mol.Biol. / Year: 1993
Title: The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.
Authors: Kalia, Y.N. / Brocklehurst, S.M. / Hipps, D.S. / Appella, E. / Sakaguchi, K. / Perham, R.N.
History
DepositionNov 25, 1992Processing site: BNL
Revision 1.0Dec 20, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4May 1, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: DIHYDROLIPOAMIDE ACETYLTRANSFERASE


Theoretical massNumber of molelcules
Total (without water)4,6081
Polymers4,6081
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)35 / -
Representative

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Components

#1: Protein/peptide DIHYDROLIPOAMIDE ACETYLTRANSFERASE


Mass: 4608.372 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
References: UniProt: P11961, dihydrolipoyl dehydrogenase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR ensembleConformers submitted total number: 35

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