Fig. 3

Sequence analysis and characterization of human OGDHc, PDHc and FAS proteins. Protein sequences were analyzed regarding PTMs, known structure, domains and flexibility. Data about PTMs were derived from PhosphoSitePlus (https://www.phosphosite.org/), known structures were datamined from the protein data bank (https://www.rcsb.org/) and manually validated. Homologous structures were identified using HHpred (https://toolkit.tuebingen.mpg.de/tools/hhpred). Domain annotations were derived from the pfam-database (https://pfam.xfam.org/). Disorder prediction was done using SPOT-disorder2 (https://sparks-lab.org/server/spot-disorder2/). Structures shown are in (A) for PDHc E2, the structures of the first (protein data bank accession code, PDB ID: 1FYC) and second (2DNE) lipoyl domain, a placeholder (from E3BP; low homology) PSBD structure (1ZY8) and the catalytic core (6H60) and the lipoyl domain of E3BP (2DNC), the PSBD (1ZY8) and core structure (6H60); in (B) a homologous lipoyl structure from PDHc E2 (1FYC) and the core of OGHDc (6H05); and in (C) the KR-domain (5C37), the acyl-carrier (PE-site; 2CG5) and the thioestarese (4Z49). The maximum distances of the disordered regions are calculated using a Cα-Cα distance of 3.8 Å. Illustrations of 3D protein models were generated using PyMOL (https://pymol.org)