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- PDB-1iyu: LIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED A... -

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Basic information

Entry
Database: PDB / ID: 1iyu
TitleLIPOYL DOMAIN OF PYRUVATE DEHYDROGENASE COMPLEX, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsDIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX
KeywordsACYLTRANSFERASE / GLYCOLYSIS / TRANSFERASE / LIPOYL
Function / homology
Function and homology information


dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / lipoic acid binding / pyruvate decarboxylation to acetyl-CoA / pyruvate dehydrogenase complex / cytoplasm
Similarity search - Function
Dihydrolipoamide acetyltransferase pyruvate dehydrogenase complex / : / 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) ...Dihydrolipoamide acetyltransferase pyruvate dehydrogenase complex / : / 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) / RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain / Biotin-requiring enzyme / Biotinyl/lipoyl domain profile. / Biotin/lipoyl attachment / Single hybrid motif / Chloramphenicol acetyltransferase-like domain superfamily / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
Similarity search - Component
Biological speciesAzotobacter vinelandii (bacteria)
MethodSOLUTION NMR
AuthorsBerg, A. / Vervoort, J. / De Kok, A.
Citation
Journal: Eur.J.Biochem. / Year: 1997
Title: Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii.
Authors: Berg, A. / Vervoort, J. / de Kok, A.
#1: Journal: J.Mol.Biol. / Year: 1996
Title: Solution Structure of the Lipoyl Domain of the 2-Oxoglutarate Dehydrogenase Complex from Azotobacter Vinelandii
Authors: Berg, A. / Vervoort, J. / De Kok, A.
#2: Journal: Eur.J.Biochem. / Year: 1995
Title: Sequential 1H and 15N Nuclear Magnetic Resonance Assignments and Secondary Structure of the Lipoyl Domain of the 2-Oxoglutarate Dehydrogenase Complex from Azotobacter Vinelandii. Evidence for ...Title: Sequential 1H and 15N Nuclear Magnetic Resonance Assignments and Secondary Structure of the Lipoyl Domain of the 2-Oxoglutarate Dehydrogenase Complex from Azotobacter Vinelandii. Evidence for High Structural Similarity with the Lipoyl Domain of the Pyruvate Dehydrogenase Complex
Authors: Berg, A. / Smits, O. / De Kok, A. / Vervoort, J.
#3: Journal: Eur.J.Biochem. / Year: 1994
Title: Sequential 1H and 15N Nuclear Magnetic Resonance Assignments and Secondary Structure of the N-Terminal Lipoyl Domain of the Dihydrolipoyl Transacetylase Component of the Pyruvate Dehydrogenase ...Title: Sequential 1H and 15N Nuclear Magnetic Resonance Assignments and Secondary Structure of the N-Terminal Lipoyl Domain of the Dihydrolipoyl Transacetylase Component of the Pyruvate Dehydrogenase Complex from Azotobacter Vinelandii
Authors: Berg, A. / De Kok, A. / Vervoort, J.
History
DepositionSep 25, 1996Processing site: BNL
Revision 1.0Mar 12, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX


Theoretical massNumber of molelcules
Total (without water)8,1731
Polymers8,1731
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX / E2P


Mass: 8173.404 Da / Num. of mol.: 1 / Fragment: LIPOYL DOMAIN, RESIDUES 1 - 79 / Source method: isolated from a natural source / Source: (natural) Azotobacter vinelandii (bacteria)
References: UniProt: P10802, dihydrolipoyllysine-residue acetyltransferase

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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

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 1

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