Structure of PDB 5k44 Chain A Binding Site BS02

Receptor Information
>5k44 Chain A (length=460) Species: 1797 (Mycolicibacterium thermoresistibile) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GDSDFVVVANRLPIDWKRSPGGLVTALEPLLRRRRGAWIGWPGIPDSDED
PIVDGDLVLYPVRLSADDVAQYYEGFSNATLWPLYHDVIVKPIYNRQWWE
RYVEVNRRFAEATSRAAARGATVWVQDYQLQLVPKMLRELRPDLTIGFFL
HIPFPPVELFMQLPWRTEITDGLLGADLVGFHLPGGAQNFLFLARRLVGA
NTSRASVGVRSKFGEVQIGSRTVKVGAFPISIDSADLDRQARQRSIRQRA
RQIRAELGNPRRILLGVDRLDYTKGIDVRLQAFAELLAEGRVNREDTVFV
QLATPSRERVEAYRLLRDDIERQVGHINGEYGEVGHPVVHYLHRPVPREE
LIAFFVAADVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAEL
GQAYLVNPHNLDHVKDTMVAALNQTPEEGRRRMRALRRQVLAHDVDLWAR
SFLDALASTR
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 chain5k44 Chain B Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5k44 Mycobacterial OtsA Structures Unveil Substrate Preference Mechanism and Allosteric Regulation by 2-Oxoglutarate and 2-Phosphoglycerate.
Resolution1.925 Å
Binding residue
(original residue number in PDB)		Y90 Y145 Q146 R286 R324
Binding residue
(residue number reindexed from 1)		Y73 Y128 Q129 R269 R307
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) H168 D385
Catalytic site (residue number reindexed from 1) H151 D368
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:5k44, PDBe:5k44, PDBj:5k44
PDBsum5k44
PubMed31772052
UniProtG7CGT2

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