Structure of PDB 1ndf Chain B

Receptor sequence
>1ndfB (length=596) Species: 10090 (Mus musculus) [Search protein sequence]
AHQDALPRLPVPPLQQSLDYYLKALQPIVSEEEWAHTKQLVDEFQTSGGV
GERLQKGLERRAKKMENWLSEWWLKTAYLQFRQPVVIYSSPGVILPKQDF
VDLQGQLRFAAKLIEGVLDFKSMIDNETLPVEFLGGQPLCMNQYYQILSS
CRVPGPKQDSVVNFLKSKRPPTHITVVHNYQFFELDVYHSDGTPLTSDQI
FVQLEKIWNSSLQSNKEPVGILTSNHRNTWAKAYNNLIKDKVNRESVNSI
QKSIFTVCLDKQVPRVSDDVYRNHVAGQMLHGGGSKFNSGNRWFDKTLQF
IVAEDGSCGMVYEHAAAEGPPIVALVDHVMEYTKKPELVRSPMVPLPMPK
KLRFNITPEIKNDIEKAKQNLSIMIQDLDIMMLTFHHFGKDFPKSEKLSP
DAFIQVALQLAYYRIYGQACATYESASLRMFHLGRTDTIRSASIDSLAFV
KGMGDSTVPEQQKVELLRKAVQAHRAYTDRAIRGEAFDRHLLGLKLQAIE
DLVSMPDIFMDTSYAIAMHFNLSTSQVPAKTDCVMFFGPVVPDGYGICYN
PMEAHINFSVSAYNSCAETNAARMAHYLEKALLDMRTLLQNHPRAK
3D structure
PDB1ndf Crystal Structure of Carnitine Acetyltransferase and Implications for the Catalytic Mechanism and Fatty Acid Transport
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y107 P120 H343 S554
Catalytic site (residue number reindexed from 1) Y78 P91 H314 S525
Enzyme Commision number 2.3.1.137: carnitine O-octanoyltransferase.
2.3.1.7: carnitine O-acetyltransferase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 152 B H343 Y452 S454 T465 S552 F566 H314 Y423 S425 T436 S523 F537
Gene Ontology
Molecular Function
GO:0003997 acyl-CoA oxidase activity
GO:0004092 carnitine O-acetyltransferase activity
GO:0008458 carnitine O-octanoyltransferase activity
GO:0016746 acyltransferase activity
Biological Process
GO:0006631 fatty acid metabolic process
GO:0019254 carnitine metabolic process, CoA-linked
GO:0033540 fatty acid beta-oxidation using acyl-CoA oxidase
GO:0046459 short-chain fatty acid metabolic process
GO:0051791 medium-chain fatty acid metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005777 peroxisome
GO:0005783 endoplasmic reticulum

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1ndf, PDBe:1ndf, PDBj:1ndf
PDBsum1ndf
PubMed12526798
UniProtP47934|CACP_MOUSE Carnitine O-acetyltransferase (Gene Name=Crat)

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