6H55
core of the human pyruvate dehydrogenase (E2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004742 | molecular_function | dihydrolipoyllysine-residue acetyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006086 | biological_process | acetyl-CoA biosynthetic process from pyruvate |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0016407 | molecular_function | acetyltransferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0034604 | molecular_function | pyruvate dehydrogenase (NAD+) activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0045254 | cellular_component | pyruvate dehydrogenase complex |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PalSPtMTMGTV |
| Chain | Residue | Details |
| A | PRO-190-VAL-179 |
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GdkInegDLIaeVETdKATvgFesleeCyM |
| Chain | Residue | Details |
| A | GLY-298-MET-269 | |
| A | GLY-171-LEU-142 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q9N0F1 |
| Chain | Residue | Details |
| A | HIS206 | |
| A | ASP210 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11181 |
| Chain | Residue | Details |
| A | ARG47 | |
| A | SER61 | |
| A | SER152 | |
| A | ASN153 | |
| A | GLY177 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER-314 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:25525879 |
| Chain | Residue | Details |
| A | LYS-282 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I |
| Chain | Residue | Details |
| A | LYS-155 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS52 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8BMF4 |
| Chain | Residue | Details |
| A | LYS59 | |
| A | LYS133 |
