3CRL
Crystal structure of the PDHK2-L2 complex.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004740 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006111 | biological_process | regulation of gluconeogenesis |
| A | 0006796 | biological_process | phosphate-containing compound metabolic process |
| A | 0006885 | biological_process | regulation of pH |
| A | 0008286 | biological_process | insulin receptor signaling pathway |
| A | 0010510 | biological_process | regulation of pyruvate decarboxylation to acetyl-CoA |
| A | 0010565 | biological_process | regulation of ketone metabolic process |
| A | 0010906 | biological_process | regulation of glucose metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0018105 | biological_process | peptidyl-serine phosphorylation |
| A | 0031670 | biological_process | cellular response to nutrient |
| A | 0034614 | biological_process | cellular response to reactive oxygen species |
| A | 0042593 | biological_process | glucose homeostasis |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0044877 | molecular_function | protein-containing complex binding |
| A | 0045254 | cellular_component | pyruvate dehydrogenase complex |
| A | 0050848 | biological_process | regulation of calcium-mediated signaling |
| A | 0072332 | biological_process | intrinsic apoptotic signaling pathway by p53 class mediator |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004740 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006111 | biological_process | regulation of gluconeogenesis |
| B | 0006796 | biological_process | phosphate-containing compound metabolic process |
| B | 0006885 | biological_process | regulation of pH |
| B | 0008286 | biological_process | insulin receptor signaling pathway |
| B | 0010510 | biological_process | regulation of pyruvate decarboxylation to acetyl-CoA |
| B | 0010565 | biological_process | regulation of ketone metabolic process |
| B | 0010906 | biological_process | regulation of glucose metabolic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0018105 | biological_process | peptidyl-serine phosphorylation |
| B | 0031670 | biological_process | cellular response to nutrient |
| B | 0034614 | biological_process | cellular response to reactive oxygen species |
| B | 0042593 | biological_process | glucose homeostasis |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0044877 | molecular_function | protein-containing complex binding |
| B | 0045254 | cellular_component | pyruvate dehydrogenase complex |
| B | 0050848 | biological_process | regulation of calcium-mediated signaling |
| B | 0072332 | biological_process | intrinsic apoptotic signaling pathway by p53 class mediator |
| C | 0006086 | biological_process | pyruvate decarboxylation to acetyl-CoA |
| C | 0045254 | cellular_component | pyruvate dehydrogenase complex |
| D | 0006086 | biological_process | pyruvate decarboxylation to acetyl-CoA |
| D | 0045254 | cellular_component | pyruvate dehydrogenase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 2000 |
| Chain | Residue |
| A | GLU251 |
| A | ASN255 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 2001 |
| Chain | Residue |
| B | ASN255 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 3001 |
| Chain | Residue |
| B | SER24 |
| B | LYS25 |
| B | PHE26 |
| B | ASN63 |
| B | TYR374 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 3002 |
| Chain | Residue |
| A | PHE26 |
| A | ASN63 |
| A | TYR374 |
| A | SER24 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ANP A 1000 |
| Chain | Residue |
| A | GLU251 |
| A | ASN255 |
| A | ARG258 |
| A | ALA259 |
| A | ASP290 |
| A | LEU303 |
| A | GLY325 |
| A | PHE326 |
| A | GLY327 |
| A | TYR328 |
| A | GLY329 |
| A | LEU330 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ANP B 1001 |
| Chain | Residue |
| B | GLU251 |
| B | ASN255 |
| B | ARG258 |
| B | ALA259 |
| B | ASP290 |
| B | LEU303 |
| B | LEU323 |
| B | GLY325 |
| B | PHE326 |
| B | GLY327 |
| B | TYR328 |
| B | GLY329 |
| B | LEU330 |
| B | PRO331 |
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 |
| C | PRO138-VAL149 |
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GekLsegDLLaeIETdKATigFevqeeGyL |
| Chain | Residue | Details |
| C | GLY157-LEU186 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q15118","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BFP9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15861126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17532006","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17683942","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25525879","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y8N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y8O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y8P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PNR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Q8I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1jm6 |
| Chain | Residue | Details |
| A | GLU251 | |
| A | HIS247 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1jm6 |
| Chain | Residue | Details |
| B | GLU251 | |
| B | HIS247 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 603 |
| Chain | Residue | Details |
| A | HIS247 | electrostatic stabiliser |
| A | GLU251 | metal ligand, proton shuttle (general acid/base) |
| A | LYS254 | metal ligand |
| A | ASN255 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 603 |
| Chain | Residue | Details |
| B | HIS247 | electrostatic stabiliser |
| B | GLU251 | metal ligand, proton shuttle (general acid/base) |
| B | LYS254 | metal ligand |
| B | ASN255 | metal ligand |
