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3HLK

Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000038biological_processvery long-chain fatty acid metabolic process
A0001676biological_processlong-chain fatty acid metabolic process
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0006631biological_processfatty acid metabolic process
A0006637biological_processacyl-CoA metabolic process
A0016790molecular_functionthiolester hydrolase activity
A0047617molecular_functionfatty acyl-CoA hydrolase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
B0000038biological_processvery long-chain fatty acid metabolic process
B0001676biological_processlong-chain fatty acid metabolic process
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005782cellular_componentperoxisomal matrix
B0005829cellular_componentcytosol
B0006631biological_processfatty acid metabolic process
B0006637biological_processacyl-CoA metabolic process
B0016790molecular_functionthiolester hydrolase activity
B0047617molecular_functionfatty acyl-CoA hydrolase activity
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000303|PubMed:19497300
ChainResidueDetails
ASER294
AASP388
AHIS422
BSER294
BASP388
BHIS422

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9QYR9
ChainResidueDetails
ALYS104
BLYS104

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9QYR9
ChainResidueDetails
ALYS470
BLYS470

220113

PDB entries from 2024-05-22

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