4EPH
CRYSTAL STRUCTURE OF RAT CARNITINE PALMITOYLTRANSFERASE 2 IN COMPLEX with CoA-site inhibitor
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 |
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 | 29 |
Details | INTRAMEM: Note=Mitochondrial inner membrane |
Chain | Residue | Details |
A | ASN179-ASN208 |
site_id | SWS_FT_FI2 |
Number of Residues | 449 |
Details | TOPO_DOM: Mitochondrial matrix |
Chain | Residue | Details |
A | ALA209-THR658 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU |
Chain | Residue | Details |
A | HIS372 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16615913, ECO:0007744|PDB:2DEB |
Chain | Residue | Details |
A | GLY452 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU |
Chain | Residue | Details |
A | TYR486 | |
A | SER488 | |
A | THR499 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52825 |
Chain | Residue | Details |
A | LYS69 | |
A | LYS85 | |
A | LYS424 | |
A | LYS439 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52825 |
Chain | Residue | Details |
A | LYS239 | |
A | LYS510 | |
A | LYS544 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52825 |
Chain | Residue | Details |
A | LYS305 |