Structure of PDB 6j5k Chain AD

Receptor sequence
>6j5kAD (length=469) Species: 9823 (Sus scrofa) [Search protein sequence]
ATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTV
RTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPI
KTKQFAAIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGA
GVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL
KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNI
FRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQ
AIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIM
DPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR
KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFY
MVGPIEEAVAKADKLAEEH
3D structure
PDB6j5k Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1.
ChainAD
Resolution6.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K164 E190 R191 R358
Catalytic site (residue number reindexed from 1) K154 E180 R181 R348
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 AD G161 G163 K164 T165 V166 Y347 G151 G153 K154 T155 V156 Y337
BS02 MG AD T165 E190 T155 E180
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process
GO:0015986 proton motive force-driven ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Cellular Component
External links
PDB RCSB:6j5k, PDBe:6j5k, PDBj:6j5k
PDBsum6j5k
PubMed31197009
UniProtK7GLT8

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