Structure of PDB 2xnd Chain B Binding Site BS01

Receptor Information
>2xnd Chain B (length=492) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEP
DNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGK
GPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELII
GDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVK
RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIY
DDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGG
GSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVG
LSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLL
SRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAF
LSHVISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA
Ligand information
Ligand IDANP
InChIInChI=1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
InChIKeyPVKSNHVPLWYQGJ-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[C@@H](O)[C@H]3O
ACDLabs 12.01O=P(O)(O)NP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(NP(=O)(O)O)O)O)O)N
FormulaC10 H17 N6 O12 P3
NamePHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
ChEMBLCHEMBL1230989
DrugBank
ZINCZINC000008660410
PDB chain2xnd Chain B Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2xnd Bioenergetic Cost of Making an Adenosine Triphosphate Molecule in Animal Mitochondria.
Resolution3.5 Å
Binding residue
(original residue number in PDB)		R171 Q172 G174 K175 T176 S177 F357 R362 Q432
Binding residue
(residue number reindexed from 1)		R153 Q154 G156 K157 T158 S159 F339 R344 Q414
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q208 K209 R373
Catalytic site (residue number reindexed from 1) K157 Q190 K191 R355
Enzyme Commision number 3.6.3.14: Transferred entry: 7.1.2.2.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0032559 adenyl ribonucleotide binding
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2xnd, PDBe:2xnd, PDBj:2xnd
PDBsum2xnd
PubMed20847295
UniProtP19483|ATPA_BOVIN ATP synthase subunit alpha, mitochondrial (Gene Name=ATP5F1A)

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