4EYW
Crystal structure of rat carnitine palmitoyltransferase 2 in complex with 1-[(R)-2-(3,4-Dihydro-1H-isoquinoline-2-carbonyl)-piperidin-1-yl]-2-phenoxy-ethanone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001676 | biological_process | long-chain fatty acid metabolic process |
| A | 0001701 | biological_process | in utero embryonic development |
| A | 0004095 | molecular_function | carnitine O-palmitoyltransferase activity |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0006853 | biological_process | carnitine shuttle |
| A | 0008458 | molecular_function | carnitine O-octanoyltransferase activity |
| A | 0009437 | biological_process | carnitine metabolic process |
| A | 0015909 | biological_process | long-chain fatty acid transport |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0070542 | biological_process | response to fatty acid |
| A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
| B | 0001676 | biological_process | long-chain fatty acid metabolic process |
| B | 0001701 | biological_process | in utero embryonic development |
| B | 0004095 | molecular_function | carnitine O-palmitoyltransferase activity |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005730 | cellular_component | nucleolus |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0006853 | biological_process | carnitine shuttle |
| B | 0008458 | molecular_function | carnitine O-octanoyltransferase activity |
| B | 0009437 | biological_process | carnitine metabolic process |
| B | 0015909 | biological_process | long-chain fatty acid transport |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0070542 | biological_process | response to fatty acid |
| B | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE L0R A 701 |
| Chain | Residue |
| A | PHE176 |
| A | THR591 |
| A | LEU212 |
| A | ASP376 |
| A | GLU487 |
| A | SER488 |
| A | CYS489 |
| A | SER490 |
| A | ALA547 |
| A | SER590 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE P6G A 702 |
| Chain | Residue |
| A | ILE446 |
| A | GLN447 |
| A | LEU592 |
| A | SER598 |
| A | LEU599 |
| A | GLY600 |
| A | ALA613 |
| A | TYR614 |
| A | CYS623 |
| A | ASN624 |
| A | HOH1252 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE L0R B 701 |
| Chain | Residue |
| B | LEU212 |
| B | ASP376 |
| B | GLU487 |
| B | SER488 |
| B | CYS489 |
| B | SER490 |
| B | THR499 |
| B | THR543 |
| B | ALA547 |
| B | HOH1219 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE P6G B 702 |
| Chain | Residue |
| B | LEU335 |
| B | GLN447 |
| B | SER590 |
| B | LEU599 |
| B | GLY600 |
| B | ALA613 |
| B | TYR614 |
| B | GLY622 |
| B | CYS623 |
| B | HOH1195 |
Functional Information from PROSITE/UniProt
| site_id | PS00439 |
| Number of Residues | 16 |
| Details | ACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPrLPIPkLeDTMkrY |
| Chain | Residue | Details |
| A | LEU49-TYR64 |
| site_id | PS00440 |
| Number of Residues | 28 |
| Details | ACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWfDKsFnLIvaeDGtaavhfEHswgDG |
| Chain | Residue | Details |
| A | ARG350-GLY377 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Intramembrane: {"description":"Note=Mitochondrial inner membrane"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 898 |
| Details | Topological domain: {"description":"Mitochondrial matrix"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17585909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RCU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16615913","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DEB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17585909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RCU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52825","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52825","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52825","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
