1NDI
Carnitine Acetyltransferase in complex with 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 | 20 |
Details | BINDING SITE FOR RESIDUE COA A 5170 |
Chain | Residue |
A | HIS343 |
A | ASP430 |
A | ALA455 |
A | SER456 |
A | THR507 |
A | ILE511 |
A | SER554 |
A | GLN555 |
A | HOH5181 |
A | HOH5219 |
A | HOH5297 |
A | GLU347 |
A | HOH5394 |
A | PRO349 |
A | LYS419 |
A | LYS423 |
A | LYS426 |
A | LEU427 |
A | SER428 |
A | PRO429 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE COA B 6170 |
Chain | Residue |
B | HIS343 |
B | GLU347 |
B | GLY348 |
B | PRO349 |
B | LYS419 |
B | LYS426 |
B | LEU427 |
B | SER428 |
B | PRO429 |
B | ASP430 |
B | ALA455 |
B | SER456 |
B | ARG504 |
B | THR507 |
B | ILE511 |
B | SER554 |
B | HOH6226 |
B | HOH6229 |
B | HOH6336 |
B | HOH6354 |
B | HOH6433 |
B | HOH6466 |
B | HOH6480 |
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 | 2 |
Details | a catalytic site defined by CSA, PubMed 12526798 |
Chain | Residue | Details |
A | SER554 | |
A | 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 |