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4EYW

Crystal structure of rat carnitine palmitoyltransferase 2 in complex with 1-[(R)-2-(3,4-Dihydro-1H-isoquinoline-2-carbonyl)-piperidin-1-yl]-2-phenoxy-ethanone

Functional Information from GO Data
ChainGOidnamespacecontents
A0001676biological_processlong-chain fatty acid metabolic process
A0001701biological_processin utero embryonic development
A0004095molecular_functioncarnitine O-palmitoyltransferase activity
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0008374molecular_functionO-acyltransferase activity
A0008458molecular_functioncarnitine O-octanoyltransferase activity
A0009437biological_processcarnitine metabolic process
A0015909biological_processlong-chain fatty acid transport
A0016746molecular_functionacyltransferase activity
A0070542biological_processresponse to fatty acid
A0120162biological_processpositive regulation of cold-induced thermogenesis
B0001676biological_processlong-chain fatty acid metabolic process
B0001701biological_processin utero embryonic development
B0004095molecular_functioncarnitine O-palmitoyltransferase activity
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0008374molecular_functionO-acyltransferase activity
B0008458molecular_functioncarnitine O-octanoyltransferase activity
B0009437biological_processcarnitine metabolic process
B0015909biological_processlong-chain fatty acid transport
B0016746molecular_functionacyltransferase activity
B0070542biological_processresponse to fatty acid
B0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE L0R A 701
ChainResidue
APHE176
ATHR591
ALEU212
AASP376
AGLU487
ASER488
ACYS489
ASER490
AALA547
ASER590

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE P6G A 702
ChainResidue
AILE446
AGLN447
ALEU592
ASER598
ALEU599
AGLY600
AALA613
ATYR614
ACYS623
AASN624
AHOH1252

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE L0R B 701
ChainResidue
BLEU212
BASP376
BGLU487
BSER488
BCYS489
BSER490
BTHR499
BTHR543
BALA547
BHOH1219

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE P6G B 702
ChainResidue
BLEU335
BGLN447
BSER590
BLEU599
BGLY600
BALA613
BTYR614
BGLY622
BCYS623
BHOH1195

Functional Information from PROSITE/UniProt
site_idPS00439
Number of Residues16
DetailsACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPrLPIPkLeDTMkrY
ChainResidueDetails
ALEU49-TYR64

site_idPS00440
Number of Residues28
DetailsACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWfDKsFnLIvaeDGtaavhfEHswgDG
ChainResidueDetails
AARG350-GLY377

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues58
DetailsINTRAMEM: Note=Mitochondrial inner membrane
ChainResidueDetails
AASN179-ASN208
BASN179-ASN208

site_idSWS_FT_FI2
Number of Residues898
DetailsTOPO_DOM: Mitochondrial matrix
ChainResidueDetails
AALA209-THR658
BALA209-THR658

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU
ChainResidueDetails
AHIS372
BHIS372

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16615913, ECO:0007744|PDB:2DEB
ChainResidueDetails
BGLY452
AGLY452

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU
ChainResidueDetails
BTYR486
BSER488
BTHR499
ATYR486
ASER488
ATHR499

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52825
ChainResidueDetails
BLYS424
BLYS439
BLYS69
BLYS85
ALYS69
ALYS85
ALYS424
ALYS439

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52825
ChainResidueDetails
ALYS544
BLYS239
BLYS510
BLYS544
ALYS510
ALYS239

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52825
ChainResidueDetails
ALYS305
BLYS305

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PDB entries from 2024-06-12

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