2H4T
Crystal structure of rat carnitine palmitoyltransferase II
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 | 2 |
| Details | BINDING SITE FOR RESIDUE D12 A 1701 |
| Chain | Residue |
| A | LEU212 |
| A | LEU592 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE D12 A 1702 |
| Chain | Residue |
| A | TYR486 |
| A | SER590 |
| A | PHE602 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE D12 A 1703 |
| Chain | Residue |
| A | CYS623 |
| A | ASN624 |
| A | GLN447 |
| A | SER598 |
| A | LEU599 |
| A | ALA613 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE D12 B 1801 |
| Chain | Residue |
| B | LEU381 |
| B | SER490 |
| B | ALA493 |
| B | THR547 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE D12 B 1802 |
| Chain | Residue |
| B | PRO133 |
| B | TYR486 |
| B | PHE602 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE D12 B 1803 |
| Chain | Residue |
| B | GLN447 |
| B | LEU592 |
| B | SER598 |
| B | LEU599 |
| B | GLY600 |
| B | ALA613 |
| B | HOH2393 |
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 | 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_FI3 |
| 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_FI4 |
| 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_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52825 |
| Chain | Residue | Details |
| A | LYS69 | |
| A | LYS85 | |
| A | LYS424 | |
| A | LYS439 | |
| B | LYS69 | |
| B | LYS85 | |
| B | LYS424 | |
| B | LYS439 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52825 |
| Chain | Residue | Details |
| A | LYS239 | |
| A | LYS510 | |
| A | LYS544 | |
| B | LYS239 | |
| B | LYS510 | |
| B | LYS544 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52825 |
| Chain | Residue | Details |
| A | LYS305 | |
| B | LYS305 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| A | HIS372 | |
| A | TYR120 | |
| A | PRO133 | |
| A | SER590 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| B | HIS372 | |
| B | TYR120 | |
| B | PRO133 | |
| B | SER590 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| A | HIS372 | |
| A | SER590 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| B | HIS372 | |
| B | SER590 |
