Structure of PDB 3oxo Chain G

Receptor sequence
>3oxoG (length=459) Species: 9823 (Sus scrofa) [Search protein sequence]
TKFYTDAVEAVKDIPNGATVLVGGFGLCGIPENLIGALLKTGVKELTAVS
NNAGVDNFGLGLLLQSKQIKRMISSYVGENAEFERQYLAGELEVELTPQG
TLAERIRAGGAGVPAFYTSTGYGTLVQEGGSPIKYNKDGSIAIASKPREV
REFNGQHFILEEAIRGDFALVKAWKADQAGNVTFRKSARNFNLPMCKAAE
TTVVEVEEIVDIGSFAPEDIHIPKIYVHRLVKGEKYEKRIERLSVIKRAA
LEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGILGLGPYPLQNEVD
ADLINAGKETVTVLPGASYFSSDESFAMIRGGHVNLTMLGAMQVSKYGDL
ANWMIPGKLVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPL
TGKQCVNRIITEKAVFDVDRKKGLTLIELWEGLTVDDIKKSTGCDFAVSP
KLIPMQQLE
3D structure
PDB3oxo Catalytic role of the conformational change in succinyl-CoA:3-oxoacid CoA transferase on binding CoA.
ChainG
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.8.3.5: 3-oxoacid CoA-transferase.
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 COA G Y76 I284 G285 I286 E305 G361 M363 N373 I376 M384 A387 A406 K407 Y76 I263 G264 I265 E284 G340 M342 N352 I355 M363 A366 A385 K386
Gene Ontology
Molecular Function
GO:0008260 succinyl-CoA:3-oxo-acid CoA-transferase activity
GO:0008410 CoA-transferase activity
GO:0016740 transferase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0006629 lipid metabolic process
GO:0046950 cellular ketone body metabolic process
GO:0046952 ketone body catabolic process
Cellular Component
GO:0005739 mitochondrion

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Molecular Function
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Cellular Component
External links
PDB RCSB:3oxo, PDBe:3oxo, PDBj:3oxo
PDBsum3oxo
PubMed20977214
UniProtQ29551|SCOT1_PIG Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (Gene Name=OXCT1)

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