Structure of PDB 6foc Chain E

Receptor sequence

>6focE (length=448) Species: 246196 (Mycolicibacterium smegmatis MC2 155)

AGRVVRITGPVVDVEFPRGSVPELFNALHAEITKTLTLEVAQHLGDSLVR
CISMQPTDGLVRGVEVTDTGASISVPVGDGVKGHVFNALGDCLDDEHWSI
HRKPPAFSDLEPMLETGLKVVDLLTPYVRGGKIALFGGAGVGKTVLIQEM
INRIARNFGGTSVFAGVGERTREGNDLWVELADANVLKDTALVFGQMDEP
PGTRMRVALSALTMAEFFRDEQGQDVLLFIDNIFRFTQAGSEVSTLLGRM
PSAVGYQPTLADEMGELQERITSTRGRSITSMQAVYVPADDYTDPAPATT
FAHLDATTELSRAVFSKGIFPAVDPLASSSTILDPAIVGDEHYRVAQEVI
RILQRYKDLQDIIAILGIDELSEEDKQLVNRARRIERFLSQNMMAAEQFT
GQPGSTVPLKETIEAFDKLTKGEFDHLPEQAFFLIGGLDDLAKKAESL

3D structure

• PDB: 6foc The structure of the catalytic domain of the ATP synthase fromMycobacterium smegmatisis a target for developing antitubercular drugs.
• Chain: E
• Resolution: 4.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K166 E192 R193 T354
• Catalytic site (residue number reindexed from 1): K143 E169 R170 T331
• 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	PO4	E	R193 R258	R170 R235

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)

External links

• PDB: RCSB:6foc, PDBe:6foc, PDBj:6foc
• PDBsum: 6foc
• PubMed: 30683723
• UniProt: A0R200|ATPB_MYCS2 ATP synthase subunit beta (Gene Name=atpD)