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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
A0006631biological_processfatty acid metabolic process
A0008458molecular_functioncarnitine O-octanoyltransferase 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
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
ALYS343

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P47934
ChainResidueDetails
AALA419
AILE423
ATHR456
ALEU504
AVAL555

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15099582
ChainResidueDetails
AMET452
ASER454
ASER465

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P47934
ChainResidueDetails
AVAL93

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P47934
ChainResidueDetails
ASER261

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AASP268

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

224004

PDB entries from 2024-08-21

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