Structure of PDB 8apb Chain D1

Receptor sequence
>8apbD1 (length=487) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
VADHKGRVGHVSQVIGAVVDVHFADGVPPVLTALDVVDKLGRDEPLTLEI
VQHLDAHTGRCIAMQTTDLLKLKAKVVSTGGNISVPVGRETLGRIFNVLG
DAIDQRGPVGEKLRMPIHAVAPKLADQAAEDAVLTTGIKVIDLILPYCKG
GKIGLFGGAGVGKTVIIMELINNVAKGHGGFSVFAGVGERTREGTDLYLE
MMQSKVIDLKGESKCVLVYGQMNEPPGARARVAQSALTMAEYFRDVEGQD
VLLFIDNIFRFTQANSEVSALLGRIPAAVGYQPTLAEDLGQLQERITSTT
KGSITSVQAVYVPADDITDPAPATTFSHLDATTVLDRAVAESGIYPAVNP
LECASRIMDPDVISVDHYNVAQDVVQMLTKYRELQDIIAVLGIDELSEED
KLIVDRARKLVKFLSQPFQVAEVFTGMTGHYVQLDDTIDSFSGLLMGTYD
QVPEMAFYMVGGINSVLEKAKKMAEEAAELEKMRRAR
3D structure
PDB8apb An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases.
ChainD1
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 D1 A185 G186 G188 K189 T190 V191 Y371 A159 G160 G162 K163 T164 V165 Y345
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8apb, PDBe:8apb, PDBj:8apb
PDBsum8apb
PubMed36220811
UniProtQ9GPE9|ATPB_TRYBB ATP synthase subunit beta, mitochondrial (Gene Name=Tb427.03.1380)

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