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1S5O

Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003997molecular_functionacyl-CoA oxidase activity
A0004092molecular_functioncarnitine O-acetyltransferase activity
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0008458molecular_functioncarnitine O-octanoyltransferase activity
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0019254biological_processcarnitine metabolic process, CoA-linked
A0033540biological_processfatty acid beta-oxidation using acyl-CoA oxidase
A0046459biological_processshort-chain fatty acid metabolic process
A0051791biological_processmedium-chain fatty acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 152 A 617
ChainResidue
ATRP81
AHIS322
AGLU326
ATYR431
ASER433
ATHR444
ASER531
APHE545
AHOH638

Functional Information from PROSITE/UniProt
site_idPS00439
Number of Residues16
DetailsACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPrLPVPpLqQSLdhY
ChainResidueDetails
ALEU14-TYR29

site_idPS00440
Number of Residues28
DetailsACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWfDKtLqFIvaeDGscglvyEHaaaEG
ChainResidueDetails
AARG300-GLY327

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P47934","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15099582","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P47934","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P47934","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
AHIS322
ATYR86
ASER533
APRO99

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
AHIS322
ASER533

239492

PDB entries from 2025-07-30

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