Fig. 3From: Unstructured regions of large enzymatic complexes control the availability of metabolites with signaling functionsSequence 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)Back to article page