Structure of PDB 5l3k Chain B Binding Site BS02

Receptor Information
>5l3k Chain B (length=458) Species: 1797 (Mycolicibacterium thermoresistibile) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SDFVVVANRLPIDLESWKRSPGGLVTALEPLLRRRRGAWIGWPGIPDSDE
DPIVLVLYPVRLSADDVAQYYEGFSNATLWPLYHDVIVKPIYNRQWWERY
VEVNRRFAEATSRAAARGATVWVQDYQLQLVPKMLRELRPDLTIGFFLHI
PFPPVELFMQLPWRTEITDGLLGADLVGFHLPGGAQNFLFLARRLVGANT
SRASVGVRSKFGEVQIGSRTVKVGAFPISIDSADLDRQARQRSIRQRARQ
IRAELGNPRRILLGVDRLDYTKGIDVRLQAFAELLAEGRVNREDTVFVQL
ATPSRERVEAYRLLRDDIERQVGHINGEYGEVGHPVVHYLHRPVPREELI
AFFVAADVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELGQ
AYLVNPHNLDHVKDTMVAALNQTPEEGRRRMRALRRQVLAHDVDLWARSF
LDALASTR
Ligand information
Ligand IDF6P
InChIInChI=1S/C6H13O9P/c7-2-6(10)5(9)4(8)3(15-6)1-14-16(11,12)13/h3-5,7-10H,1-2H2,(H2,11,12,13)/t3-,4-,5+,6-/m1/s1
InChIKeyBGWGXPAPYGQALX-ARQDHWQXSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCC1OC(O)(CO)C(O)C1O
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)(CO)O)O)O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@](O1)(CO)O)O)O)OP(=O)(O)O
CACTVS 3.341OC[C]1(O)O[CH](CO[P](O)(O)=O)[CH](O)[CH]1O
CACTVS 3.341OC[C@@]1(O)O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@@H]1O
FormulaC6 H13 O9 P
Name6-O-phosphono-beta-D-fructofuranose;
FRUCTOSE-6-PHOSPHATE;
6-O-phosphono-beta-D-fructose;
6-O-phosphono-D-fructose;
6-O-phosphono-fructose
ChEMBLCHEMBL604196
DrugBank
ZINCZINC000004096690
PDB chain5l3k Chain B Residue 502 [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)		R18 Y90 D144 R286 R324
Binding residue
(residue number reindexed from 1)		R9 Y71 D125 R267 R305
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) H168 D385
Catalytic site (residue number reindexed from 1) H149 D366
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5l3k, PDBe:5l3k, PDBj:5l3k
PDBsum5l3k
PubMed31772052
UniProtA0A117IMA6

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