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1NDF

Carnitine Acetyltransferase in Complex with Carnitine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003997molecular_functionacyl-CoA oxidase activity
A0004092molecular_functioncarnitine O-acetyltransferase activity
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005777cellular_componentperoxisome
A0005783cellular_componentendoplasmic reticulum
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
B0003997molecular_functionacyl-CoA oxidase activity
B0004092molecular_functioncarnitine O-acetyltransferase activity
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005777cellular_componentperoxisome
B0005783cellular_componentendoplasmic reticulum
B0006631biological_processfatty acid metabolic process
B0008458molecular_functioncarnitine O-octanoyltransferase activity
B0016746molecular_functionacyltransferase activity
B0019254biological_processcarnitine metabolic process, CoA-linked
B0033540biological_processfatty acid beta-oxidation using acyl-CoA oxidase
B0046459biological_processshort-chain fatty acid metabolic process
B0051791biological_processmedium-chain fatty acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 152 A 5001
ChainResidue
ATRP102
AHOH5044
AHIS343
AGLU347
ATYR452
ASER454
ATHR465
ASER552
APHE566
AHOH5025

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 152 B 6001
ChainResidue
BTRP102
BHIS343
BGLU347
BTYR452
BSER454
BTHR465
BSER552
BPHE566
BHOH6007
BHOH6261

Functional Information from PROSITE/UniProt
site_idPS00439
Number of Residues16
DetailsACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPrLPVPpLqQSLdyY
ChainResidueDetails
ALEU35-TYR50

site_idPS00440
Number of Residues28
DetailsACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWfDKtLqFIvaeDGscgmvyEHaaaEG
ChainResidueDetails
AARG321-GLY348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS343
BHIS343

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:12526798, ECO:0000269|PubMed:15155726
ChainResidueDetails
ALYS419
BSER454
BSER456
BTHR465
BARG504
BGLN555
ATYR452
ASER454
ASER456
ATHR465
AARG504
AGLN555
BLYS419
BTYR452

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS423
BLYS423

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS93
BLYS93

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS261
BLYS261

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P43155
ChainResidueDetails
ALYS268
BLYS268

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
ATYR107
ASER554
APRO120
AHIS343

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
BTYR107
BSER554
BPRO120
BHIS343

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
ASER554
AHIS343

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
BSER554
BHIS343

site_idMCSA1
Number of Residues4
DetailsM-CSA 629
ChainResidueDetails
ATYR107steric role
APRO120steric role
AHIS343hydrogen bond acceptor, proton acceptor, proton donor
ASER554electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 629
ChainResidueDetails
BTYR107steric role
BPRO120steric role
BHIS343hydrogen bond acceptor, proton acceptor, proton donor
BSER554electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-07-10

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