Structure of PDB 7njr Chain F

Receptor sequence
>7njrF (length=468) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
TAGRVVRITGPVVDVEFPRGSVPELFNALHAEITFGALAKTLTLEVAQHL
GDSLVRCISMQPTDGLVRGVEVTDTGASISVPVGDGVKGHVFNALGDCLD
DPGYGKDFEHWSIHRKPPAFSDLEPRTEMLETGLKVVDLLTPYVRGGKIA
LFGGAGVGKTVLIQEMINRIARNFGGTSVFAGVGERTREGNDLWVELADA
NVLKDTALVFGQMDEPPGTRMRVALSALTMAEFFRDEQGQDVLLFIDNIF
RFTQAGSEVSTLLGRMPSAVGYQPTLADEMGELQERITSTRGRSITSMQA
VYVPADDYTDPAPATTFAHLDATTELSRAVFSKGIFPAVDPLASSSTILD
PAIVGDEHYRVAQEVIRILQRYKDLQDIIAILGIDELSEEDKQLVNRARR
IERFLSQNMMAAEQFTGQPGSTVPLKETIEAFDKLTKGEFDHLPEQAFFL
IGGLDDLAKKAESLGAKL
3D structure
PDB7njr Structure of the ATP synthase from Mycobacterium smegmatis provides targets for treating tuberculosis.
ChainF
Resolution2.56 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 ATP F G163 G165 K166 T167 V168 R193 F343 A419 F422 G156 G158 K159 T160 V161 R186 F336 A412 F415
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:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0045259 proton-transporting ATP synthase complex
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:7njr, PDBe:7njr, PDBj:7njr
PDBsum7njr
PubMed34782468
UniProtA0R200|ATPB_MYCS2 ATP synthase subunit beta (Gene Name=atpD)

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