Structure of PDB 8rth Chain E

Receptor sequence
>8rthE (length=666) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
DFKKVLVANRGEIACRVFRTCREMNIRTVAVCCEGEPNAKHVLEADEAFV
LGPPPASTSYLRGDRIICAAKKLQADAVHPGYGFLSENAEFASAVLAAGL
KFVGPPPAAMLSMGSKSESKRIMEAAGVPIVPGYYGEDQNPDRLLHEAKT
IGFPVLIKAVSGGGGKGMKIVMEETEFHLMLESAKREAINFFKDDRVILE
RYVMHPRHIECQIFFDSFGNGVFFFERDCSVQRRHQKVIEEAPAPGLSVD
MRRRIGDVALTAARAVGYVGAGTVEFIFDTEKDEFFFMEMNTRLQVEHPV
TEQCQVRGRPLDLVRLQLQTAMGLPLGFRQEDISMSGASVEARIYAESPR
NGFLPVGGRLRYLKEPPQGNRGTVKVRLDTGFRAGDDVLVHYDPMIAKLV
VWGDNRATALEGLRTALASYHIVGVETNIDFLQCCLSNPGFVEGGVTTRF
IEDNSVNLLQPREIPNNVLALAAVSYLCSQRGTSTLFWPNRQISQGVCFT
VGGNPVVVRVTVSTKMCFTCDFDSSSVTVYVESTTNMPDSSTFIRVTVDG
ETRFGFTSFVTDSEVAVALPQGFYTLALQPLATDFGSTSAQANGSASVLS
PMPGKVTKLLVADGTLVQQGQAILILEAMKMEHVVKASCDGEVKFCVHAD
GIVGGSTLLAHIASAA
3D structure
PDB8rth The cryo-EM structure of trypanosome 3-methylcrotonyl-CoA carboxylase provides mechanistic and dynamic insights into its enzymatic function
ChainE
Resolution2.37 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 E M640 K641 M629 K630
Gene Ontology
Molecular Function
GO:0004485 methylcrotonoyl-CoA carboxylase activity
GO:0005524 ATP binding
GO:0009374 biotin binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0019856 pyrimidine nucleobase biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005929 cilium

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8rth, PDBe:8rth, PDBj:8rth
PDBsum8rth
PubMed38593794
UniProtQ57YQ4

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