Structure of PDB 5jio Chain A Binding Site BS02

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 IDG6P
InChIInChI=1S/C6H13O9P/c7-3-2(1-14-16(11,12)13)15-6(10)5(9)4(3)8/h2-10H,1H2,(H2,11,12,13)/t2-,3-,4+,5-,6+/m1/s1
InChIKeyNBSCHQHZLSJFNQ-DVKNGEFBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)OP(=O)(O)O
CACTVS 3.341O[CH]1O[CH](CO[P](O)(O)=O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341O[C@H]1O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H](O)[C@H]1O
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)OP(=O)(O)O
ACDLabs 10.04O=P(O)(O)OCC1OC(O)C(O)C(O)C1O
FormulaC6 H13 O9 P
Name6-O-phosphono-alpha-D-glucopyranose;
ALPHA-D-GLUCOSE-6-PHOSPHATE;
6-O-phosphono-alpha-D-glucose;
6-O-phosphono-D-glucose;
6-O-phosphono-glucose
ChEMBL
DrugBankDB02007
ZINCZINC000003875375
PDB chain5jio Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		R18 P37 G38 Y90 D144 R324
Binding residue
(residue number reindexed from 1)		R12 P27 G28 Y80 D134 R314
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

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

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