2H3U
Crystal structure of murine carnitine acetyltransferase in complex with carnitine and CoA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003997 | molecular_function | acyl-CoA oxidase activity |
A | 0004092 | molecular_function | carnitine O-acetyltransferase activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0005777 | cellular_component | peroxisome |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0008458 | molecular_function | carnitine O-octanoyltransferase activity |
A | 0016020 | cellular_component | membrane |
A | 0016740 | molecular_function | transferase activity |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0019254 | biological_process | carnitine metabolic process, CoA-linked |
A | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
A | 0046459 | biological_process | short-chain fatty acid metabolic process |
A | 0051791 | biological_process | medium-chain fatty acid metabolic process |
B | 0003997 | molecular_function | acyl-CoA oxidase activity |
B | 0004092 | molecular_function | carnitine O-acetyltransferase activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0005777 | cellular_component | peroxisome |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0008458 | molecular_function | carnitine O-octanoyltransferase activity |
B | 0016020 | cellular_component | membrane |
B | 0016740 | molecular_function | transferase activity |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0019254 | biological_process | carnitine metabolic process, CoA-linked |
B | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
B | 0046459 | biological_process | short-chain fatty acid metabolic process |
B | 0051791 | biological_process | medium-chain fatty acid metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE COA A 1802 |
Chain | Residue |
A | LEU163 |
A | PRO429 |
A | ASP430 |
A | SER454 |
A | ALA455 |
A | SER456 |
A | ARG504 |
A | THR507 |
A | ILE511 |
A | GLN555 |
A | 1521801 |
A | GLU347 |
A | HOH1856 |
A | HOH1885 |
A | HOH1902 |
A | HOH1909 |
A | HOH1991 |
A | HOH2007 |
A | HOH2076 |
A | HOH2173 |
A | HOH2211 |
A | HOH2298 |
A | GLY348 |
A | HOH2366 |
A | HOH2449 |
A | HOH2462 |
A | HOH2469 |
A | HOH2485 |
A | PRO349 |
A | LYS419 |
A | LYS423 |
A | LYS426 |
A | LEU427 |
A | SER428 |
site_id | AC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE COA B 1902 |
Chain | Residue |
B | GLY348 |
B | PRO349 |
B | LYS419 |
B | LYS423 |
B | LYS426 |
B | LEU427 |
B | SER428 |
B | PRO429 |
B | ASP430 |
B | ALA455 |
B | SER456 |
B | ARG504 |
B | THR507 |
B | ILE511 |
B | GLN555 |
B | VAL556 |
B | 1521901 |
B | HOH2002 |
B | HOH2081 |
B | HOH2096 |
B | HOH2112 |
B | HOH2170 |
B | HOH2172 |
B | HOH2443 |
B | HOH2447 |
B | HOH2595 |
B | HOH2681 |
B | HOH2785 |
B | HOH2820 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 152 A 1801 |
Chain | Residue |
A | TRP102 |
A | HIS343 |
A | TYR452 |
A | SER454 |
A | THR465 |
A | SER552 |
A | PHE566 |
A | VAL569 |
A | COA1802 |
A | HOH1825 |
A | HOH2366 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 152 B 1901 |
Chain | Residue |
B | TRP102 |
B | HIS343 |
B | TYR452 |
B | SER454 |
B | THR465 |
B | SER552 |
B | PHE566 |
B | VAL569 |
B | COA1902 |
B | HOH1912 |
B | HOH2511 |
B | HOH2681 |
Functional Information from PROSITE/UniProt
site_id | PS00439 |
Number of Residues | 16 |
Details | ACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPrLPVPpLqQSLdyY |
Chain | Residue | Details |
A | LEU35-TYR50 |
site_id | PS00440 |
Number of Residues | 28 |
Details | ACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWfDKtLqFIvaeDGscgmvyEHaaaEG |
Chain | Residue | Details |
A | ARG321-GLY348 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS343 | |
B | HIS343 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12526798, ECO:0000269|PubMed:15155726 |
Chain | Residue | Details |
A | LYS419 | |
B | SER454 | |
B | SER456 | |
B | THR465 | |
B | ARG504 | |
B | GLN555 | |
A | TYR452 | |
A | SER454 | |
A | SER456 | |
A | THR465 | |
A | ARG504 | |
A | GLN555 | |
B | LYS419 | |
B | TYR452 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS423 | |
B | LYS423 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS93 | |
B | LYS93 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS261 | |
B | LYS261 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P43155 |
Chain | Residue | Details |
A | LYS268 | |
B | LYS268 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 629 |
Chain | Residue | Details |
A | TYR107 | steric role |
A | PRO120 | steric role |
A | HIS343 | hydrogen bond acceptor, proton acceptor, proton donor |
A | SER554 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 629 |
Chain | Residue | Details |
B | TYR107 | steric role |
B | PRO120 | steric role |
B | HIS343 | hydrogen bond acceptor, proton acceptor, proton donor |
B | SER554 | electrostatic stabiliser, hydrogen bond donor |