Structure of PDB 5l3k Chain A Binding Site BS01

Receptor Information
>5l3k Chain A (length=448) Species: 1797 (Mycolicibacterium thermoresistibile) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SDFVVVANRLPIDLRSPGGLVTALEPLLRRAWIGWPGIPDSDEDPVLYPV
RLSADDVAQYYEGFSNATLWPLYHDVIVKPIYNRQWWERYVEVNRRFAEA
TSRAAARGATVWVQDYQLQLVPKMLRELRPDLTIGFFLHIPFPPVELFMQ
LPWRTEITDGLLGADLVGFHLPGGAQNFLFLARRLVGANTSRASVGVRSK
FGEVQIGSRTVKVGAFPISIDSADLDRQARQRSIRQRARQIRAELGNPRR
ILLGVDRLDYTKGIDVRLQAFAELLAEGRVNREDTVFVQLATPSRERVEA
YRLLRDDIERQVGHINGEYGEVGHPVVHYLHRPVPREELIAFFVAADVML
VTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELGQAYLVNPHNLD
HVKDTMVAALNQTPEEGRRRMRALRRQVLAHDVDLWARSFLDALASTR
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 chain5l3k Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5l3k Mycobacterial OtsA Structures Unveil Substrate Preference Mechanism and Allosteric Regulation by 2-Oxoglutarate and 2-Phosphoglycerate.
Resolution2.305 Å
Binding residue
(original residue number in PDB)		G38 G39 D285 R286 K291 L319 T321 V363 N388 L389 V390 E393
Binding residue
(residue number reindexed from 1)		G18 G19 D256 R257 K262 L290 T292 V334 N359 L360 V361 E364
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H168 D385
Catalytic site (residue number reindexed from 1) H139 D356
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:5l3k, PDBe:5l3k, PDBj:5l3k
PDBsum5l3k
PubMed31772052
UniProtA0A117IMA6

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