Structure of PDB 6foc Chain F Binding Site BS02

Receptor Information
>6foc Chain F (length=454) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TAGRVVRITGPVVDVEFPRGSVPELFNALHAEITKTLTLEVAQHLGDSLV
RCISMQPTDGLVRGVEVTDTGASISVPVGDGVKGHVFNALGDCLDDDFEH
WSIHRKPPAFSDLEPRTEMLETGLKVVDLLTPYVRGGKIALFGGAGVGKT
VLIQEMINRIARNFGGTSVFAGVGERTREGNDLWVELADANVLKDTALVF
GQMDEPPGTRMRVALSALTMAEFFRDEQGQDVLLFIDNIFRFTQAGSEVS
TLLGRMPSAVGYQPTLADEMGELQERITSTRGRSITSMQAVYVPADDYTD
PAPATTFAHLDATTELSRAVFSKGIFPAVDPLASSSTILDPAIVGDEHYR
VAQEVIRILQRYKDLQDIIAILGIDELSEEDKQLVNRARRIERFLSQNMM
AAEQFTGQPGSTVPLKETIEAFDKLTKGEFDHLPEQAFFLIGGLDDLAKK
AESL
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain6foc Chain F Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6foc The structure of the catalytic domain of the ATP synthase fromMycobacterium smegmatisis a target for developing antitubercular drugs.
Resolution4.0 Å
Binding residue
(original residue number in PDB)		G163 V164 G165 K166 T167 V168 F343 F422
Binding residue
(residue number reindexed from 1)		G146 V147 G148 K149 T150 V151 F326 F405
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K166 E192 R193 T354
Catalytic site (residue number reindexed from 1) K149 E175 R176 T337
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
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:6foc, PDBe:6foc, PDBj:6foc
PDBsum6foc
PubMed30683723
UniProtA0R200|ATPB_MYCS2 ATP synthase subunit beta (Gene Name=atpD)

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