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1DXL

Dihydrolipoamide dehydrogenase of glycine decarboxylase from Pisum Sativum

Summary for 1DXL
Entry DOI10.2210/pdb1dxl/pdb
Related1LPF 1LVL 1OJT 3LAD
DescriptorDIHYDROLIPOAMIDE DEHYDROGENASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
Functional Keywordsoxidoreductase, dihydrolipoamide dehydrogenase, multienzyme complex protein, pyruvate dehydrogenase complex, glycine decarboxylase complex, flavoprotein
Biological sourcePISUM SATIVUM (PEA)
Cellular locationMitochondrion matrix: P31023
Total number of polymer chains4
Total formula weight202378.04
Authors
Faure, M.,Cohen-Addad, C.,Bourguignon, J.,Macherel, D.,Neuburger, M.,Douce, R. (deposition date: 2000-01-10, release date: 2000-07-20, Last modification date: 2023-12-06)
Primary citationFaure, M.,Bourguignon, J.,Neuburger, M.,Macherel, D.,Sieker, L.,Ober, R.,Kahn, R.,Cohen-Addad, C.,Douce, R.
Interaction between the Lipoamide-Containing H-Protein and the Lipoamide Dehydrogenase (L-Protein) of the Glycine Decarboxylase Multienzyme System. 2. Crystal Structure of H- and L-Proteins
Eur.J.Biochem., 267:2890-, 2000
Cited by
PubMed: 10806386
DOI: 10.1046/J.1432-1033.2000.01330.X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.15 Å)
Structure validation

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