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2FW3

Crystal structure of rat carnitine palmitoyltransferase 2 in complex with antidiabetic drug ST1326

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
A0006629biological_processlipid metabolic process
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
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0070542biological_processresponse to fatty acid
A0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BUI A 900
ChainResidue
AHIS372
AALA613
AGLY622
ACYS623
AHOH988
AGLN447
ATYR486
ASER488
ATHR499
ASER588
ASER590
APHE602
AVAL605

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 Residues29
DetailsINTRAMEM: Note=Mitochondrial inner membrane
ChainResidueDetails
AASN179-ASN208

site_idSWS_FT_FI2
Number of Residues449
DetailsTOPO_DOM: Mitochondrial matrix
ChainResidueDetails
AALA209-THR658

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU
ChainResidueDetails
AHIS372

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16615913, ECO:0007744|PDB:2DEB
ChainResidueDetails
AGLY452

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17585909, ECO:0007744|PDB:2RCU
ChainResidueDetails
ATYR486
ASER488
ATHR499

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52825
ChainResidueDetails
ALYS439
ALYS69
ALYS85
ALYS424

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52825
ChainResidueDetails
ALYS510
ALYS544
ALYS239

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52825
ChainResidueDetails
ALYS305

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PDB entries from 2024-04-17

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