Structure of PDB 8apj Chain E1

Receptor sequence
>8apjE1 (length=486) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
ADHKGRVGHVSQVIGAVVDVHFADGVPPVLTALDVVDKLGRDEPLTLEIV
QHLDAHTGRCIAMQTTDLLKLKAKVVSTGGNISVPVGRETLGRIFNVLGD
AIDQRGPVGEKLRMPIHAVAPKLADQAAEDAVLTTGIKVIDLILPYCKGG
KIGLFGGAGVGKTVIIMELINNVAKGHGGFSVFAGVGERTREGTDLYLEM
MQSKVIDLKGESKCVLVYGQMNEPPGARARVAQSALTMAEYFRDVEGQDV
LLFIDNIFRFTQANSEVSALLGRIPAAVGYQPTLAEDLGQLQERITSTTK
GSITSVQAVYVPADDITDPAPATTFSHLDATTVLDRAVAESGIYPAVNPL
ECASRIMDPDVISVDHYNVAQDVVQMLTKYRELQDIIAVLGIDELSEEDK
LIVDRARKLVKFLSQPFQVAEVFTGMTGHYVQLDDTIDSFSGLLMGTYDQ
VPEMAFYMVGGINSVLEKAKKMAEEAAELEKMRRAR
3D structure
PDB8apj An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases.
ChainE1
Resolution3.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
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 ADP E1 G186 G188 K189 T190 V191 Y371 F450 G159 G161 K162 T163 V164 Y344 F423
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Cellular Component
External links
PDB RCSB:8apj, PDBe:8apj, PDBj:8apj
PDBsum8apj
PubMed36220811
UniProtQ9GPE9|ATPB_TRYBB ATP synthase subunit beta, mitochondrial (Gene Name=Tb427.03.1380)

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