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 | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0008374 | molecular_function | O-acyltransferase activity |
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 | 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 | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0008374 | molecular_function | O-acyltransferase activity |
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 | 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 | INTRAMEM: Note=Mitochondrial inner membrane |
Chain | Residue | Details |
A | ASN179-ASN208 | |
B | ASN179-ASN208 |
site_id | SWS_FT_FI2 |
Number of Residues | 898 |
Details | TOPO_DOM: Mitochondrial matrix |
Chain | Residue | Details |
A | ALA209-THR658 | |
B | ALA209-THR658 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU |
Chain | Residue | Details |
A | HIS372 | |
B | HIS372 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16615913, ECO:0007744|PDB:2DEB |
Chain | Residue | Details |
B | GLY452 | |
A | GLY452 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU |
Chain | Residue | Details |
B | TYR486 | |
B | SER488 | |
B | THR499 | |
A | TYR486 | |
A | SER488 | |
A | THR499 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52825 |
Chain | Residue | Details |
B | LYS424 | |
B | LYS439 | |
B | LYS69 | |
B | LYS85 | |
A | LYS69 | |
A | LYS85 | |
A | LYS424 | |
A | LYS439 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52825 |
Chain | Residue | Details |
A | LYS544 | |
B | LYS239 | |
B | LYS510 | |
B | LYS544 | |
A | LYS510 | |
A | LYS239 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52825 |
Chain | Residue | Details |
A | LYS305 | |
B | LYS305 |