Structure of PDB 8sgy Chain V

Receptor sequence
>8sgyV (length=657) Species: 5689 (Leishmania tarentolae) [Search protein sequence]
VLVANRGEIACRVMATCRRLGIKTVAVYSTADEQAKHVKVADESVCIGPP
ASVESYLCIDKIVDACKKTGAQAVHPGYGFLSENGEFQSALQKNNIVFVG
PDAHSIESMGDKIESKRLAQRAGVTCIPGFIGEVKTHEDLLRFAREIGYP
VMIKASGGGGGKGMRVAYNDTQCVEYYDMCREEAKAAFHSDKMLVERFID
HPRHIEIQVIADRRGNTVYLPERECSIQRRNQKVIEEAPSVLLDATTRKA
MGEEAVAMARAVQYVSAGTVENVVNPQKQFYFLEMNTRLQVEHPITEEIT
GVDLVEQMLRAAADLPLSITQDDITINGHATECRVYAEDPMKNYFPSIGR
LTMYQEPTGAGVRCDSGIIEGSQISVYYDPLICKLSTWGRDRAECIGRME
KALDEYVIRGLRHNICLLRDVVTEPRYRSGSITTNYLQEQYPNGFKKAEL
TAEEMQLMYEVAACVHLKRERLHYTQGTAPSERQLYLSVGAGQEGETPVY
VRYLDDSHFEIGASKHGPFRKMEVVWKASYPIIRVKDGEAETVLQFWGTN
EVTYGMQMRGTTFDVNVMSDLQSTLAHFVPITEATTNTKQILSPMPGVIV
AIKVQPGQMVVAGEELLTLEAMKMRNKIHAQADGKVKEVKVKLGATVEDN
EVLVELE
3D structure
PDB8sgy CryoEM reveals oligomeric isomers of a multienzyme complex and assembly mechanics.
ChainV
Resolution8.62 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.4.1.3: propionyl-CoA carboxylase.
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 BTI V M630 K631 M622 K623
Gene Ontology
Molecular Function
GO:0004658 propionyl-CoA carboxylase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8sgy, PDBe:8sgy, PDBj:8sgy
PDBsum8sgy
PubMed37128595
UniProtA0A640KC69

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