Structure of PDB 5jio Chain A Binding Site BS01

Receptor Information
>5jio Chain A (length=467) Species: 1797 (Mycolicibacterium thermoresistibile) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SGDSDFVVVANRLPIDLERTTSWKRSPGGLVTALEPLLRRRRGAWIGWPG
IPDSDEDPIVDGDLVLYPVRLSADDVAQYYEGFSNATLWPLYHDVIVKPI
YNRQWWERYVEVNRRFAEATSRAAARGATVWVQDYQLQLVPKMLRELRPD
LTIGFFLHIPFPPVELFMQLPWRTEITDGLLGADLVGFHLPGGAQNFLFL
ARRLVGANTSRASVGVRSKFGEVQIGSRTVKVGAFPISIDSADLDRQARQ
RSIRQRARQIRAELGNPRRILLGVDRLDYTKGIDVRLQAFAELLAEGRVN
REDTVFVQLATPSRERVEAYRLLRDDIERQVGHINGEYGEVGHPVVHYLH
RPVPREELIAFFVAADVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEF
TGAAAELGQAYLVNPHNLDHVKDTMVAALNQTPEEGRRRMRALRRQVLAH
DVDLWARSFLDALASTR
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 chain5jio Chain A Residue 501 [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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PDB5jio Mycobacterial OtsA Structures Unveil Substrate Preference Mechanism and Allosteric Regulation by 2-Oxoglutarate and 2-Phosphoglycerate.
Resolution1.711 Å
Binding residue
(original residue number in PDB)		G38 G39 T42 V284 D285 R286 K291 L319 T321 V363 R365 L368 L389 V390 E393
Binding residue
(residue number reindexed from 1)		G28 G29 T32 V274 D275 R276 K281 L309 T311 V353 R355 L358 L379 V380 E383
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H168 D385
Catalytic site (residue number reindexed from 1) H158 D375
Enzyme Commision number 2.4.1.347: alpha,alpha-trehalose-phosphate synthase (ADP-forming).
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005992 trehalose biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5jio, PDBe:5jio, PDBj:5jio
PDBsum5jio
PubMed31772052
UniProtG7CGT2

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