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2H4T

Crystal structure of rat carnitine palmitoyltransferase II

Functional Information from GO Data
ChainGOidnamespacecontents
A0001676biological_processlong-chain fatty acid metabolic process
A0001701biological_processin utero embryonic development
A0004095molecular_functioncarnitine O-palmitoyltransferase activity
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006635biological_processfatty acid beta-oxidation
A0006853biological_processcarnitine shuttle
A0008458molecular_functioncarnitine O-octanoyltransferase activity
A0009437biological_processcarnitine metabolic process
A0015909biological_processlong-chain fatty acid transport
A0016740molecular_functiontransferase activity
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
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005759cellular_componentmitochondrial matrix
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006635biological_processfatty acid beta-oxidation
B0006853biological_processcarnitine shuttle
B0008458molecular_functioncarnitine O-octanoyltransferase activity
B0009437biological_processcarnitine metabolic process
B0015909biological_processlong-chain fatty acid transport
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0070542biological_processresponse to fatty acid
B0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE D12 A 1701
ChainResidue
ALEU212
ALEU592

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE D12 A 1702
ChainResidue
ATYR486
ASER590
APHE602

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE D12 A 1703
ChainResidue
ACYS623
AASN624
AGLN447
ASER598
ALEU599
AALA613

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE D12 B 1801
ChainResidue
BLEU381
BSER490
BALA493
BTHR547

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE D12 B 1802
ChainResidue
BPRO133
BTYR486
BPHE602

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE D12 B 1803
ChainResidue
BGLN447
BLEU592
BSER598
BLEU599
BGLY600
BALA613
BHOH2393

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
DetailsIntramembrane: {"description":"Note=Mitochondrial inner membrane"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17585909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RCU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16615913","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2DEB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17585909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RCU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52825","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52825","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52825","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
AHIS372
ATYR120
APRO133
ASER590

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
BHIS372
BTYR120
BPRO133
BSER590

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
AHIS372
ASER590

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1q6x
ChainResidueDetails
BHIS372
BSER590

244693

PDB entries from 2025-11-12

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