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 | 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 | 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 | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12526798","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15155726","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P43155","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| A | TYR107 | |
| A | SER554 | |
| A | PRO120 | |
| A | HIS343 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| B | TYR107 | |
| B | SER554 | |
| B | PRO120 | |
| B | HIS343 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| A | SER554 | |
| A | HIS343 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| B | SER554 | |
| B | HIS343 |
| 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 |
