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1B5S

DIHYDROLIPOYL TRANSACETYLASE (E.C.2.3.1.12) CATALYTIC DOMAIN (RESIDUES 184-425) FROM BACILLUS STEAROTHERMOPHILUS

Summary for 1B5S
Entry DOI10.2210/pdb1b5s/pdb
DescriptorDIHYDROLIPOAMIDE ACETYLTRANSFERASE (1 entity in total)
Functional Keywordsdihydrolipoyl transacetylase, pyruvate dehydrogenase, e2p, dihydrolipoyl acetyltransferase, acyltransferase
Biological sourceGeobacillus stearothermophilus
Total number of polymer chains5
Total formula weight132183.92
Authors
Izard, T.,Aevarsson, A.,Allen, M.D.,Westphal, A.H.,Perham, R.N.,De Kok, A.,Hol, W.G. (deposition date: 1999-01-10, release date: 1999-02-16, Last modification date: 2023-08-02)
Primary citationIzard, T.,Aevarsson, A.,Allen, M.D.,Westphal, A.H.,Perham, R.N.,de Kok, A.,Hol, W.G.
Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes.
Proc.Natl.Acad.Sci.USA, 96:1240-1245, 1999
Cited by
PubMed: 9990008
DOI: 10.1073/pnas.96.4.1240
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.4 Å)
Structure validation

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