Structure of PDB 7njp Chain F

Receptor sequence
>7njpF (length=469) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
KTAGRVVRITGPVVDVEFPRGSVPELFNALHAEITFGALAKTLTLEVAQH
LGDSLVRCISMQPTDGLVRGVEVTDTGASISVPVGDGVKGHVFNALGDCL
DDPGYGKDFEHWSIHRKPPAFSDLEPRTEMLETGLKVVDLLTPYVRGGKI
ALFGGAGVGKTVLIQEMINRIARNFGGTSVFAGVGERTREGNDLWVELAD
ANVLKDTALVFGQMDEPPGTRMRVALSALTMAEFFRDEQGQDVLLFIDNI
FRFTQAGSEVSTLLGRMPSAVGYQPTLADEMGELQERITSTRGRSITSMQ
AVYVPADDYTDPAPATTFAHLDATTELSRAVFSKGIFPAVDPLASSSTIL
DPAIVGDEHYRVAQEVIRILQRYKDLQDIIAILGIDELSEEDKQLVNRAR
RIERFLSQNMMAAEQFTGQPGSTVPLKETIEAFDKLTKGEFDHLPEQAFF
LIGGLDDLAKKAESLGAKL
3D structure
PDB7njp Structure of the ATP synthase from Mycobacterium smegmatis provides targets for treating tuberculosis.
ChainF
Resolution2.84 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 G157 G159 K160 T161 V162 R187 F337 A413 F416
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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Biological Process
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Cellular Component
External links
PDB RCSB:7njp, PDBe:7njp, PDBj:7njp
PDBsum7njp
PubMed34782468
UniProtA0R200|ATPB_MYCS2 ATP synthase subunit beta (Gene Name=atpD)

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