2RCU
Crystal structure of rat carnitine palmitoyltransferase 2 in complex with r-3-(hexadecanoylamino)-4-(trimethylazaniumyl)butanoate
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 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 |
| A | GLY452 | |
| B | GLY452 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU |
| Chain | Residue | Details |
| A | TYR486 | |
| A | SER488 | |
| A | THR499 | |
| B | TYR486 | |
| B | SER488 | |
| B | 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 | |
| A | LYS69 | |
| A | LYS85 | |
| A | LYS424 | |
| A | LYS439 | |
| B | LYS69 | |
| B | LYS85 |
| 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 | LYS239 | |
| A | LYS510 |
| 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 |
