Structure of PDB 5o5e Chain A Binding Site BS02

Receptor Information
>5o5e Chain A (length=381) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNKTSRQQIPES
QGVISGAVFLIILFCFIPFPFLPHHEFVALIGALLAICCMIFLGFADDVL
NLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPKPFRPILLDLGILYYV
YMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDH
VFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAGVGILGHF
SKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLNIKTGKLEMSYSKF
KTKSLSFLGTFILKVAESLQLVTVHQSETEDGEFTECNNMTLINLLLKVL
GPIHERNLTLLLLLLQILGSAITFSIRYQLV
Ligand information
Ligand ID9LH
InChIInChI=1S/C38H62N4O16/c1-19(2)13-11-9-7-5-4-6-8-10-12-14-24(46)40-27-31(51)28(48)22(55-37(27)58-36-26(39-20(3)44)30(50)29(49)23(18-43)56-36)17-21(45)34-32(52)33(53)35(57-34)42-16-15-25(47)41-38(42)54/h12,14-16,19,21-23,26-37,43,45,48-53H,4-11,13,17-18H2,1-3H3,(H,39,44)(H,40,46)(H,41,47,54)/b14-12+/t21-,22-,23-,26-,27-,28+,29-,30-,31-,32+,33-,34-,35-,36-,37+/m1/s1
InChIKeyMEYZYGMYMLNUHJ-DIRMKAHISA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC(C)CCCCCCCCCC=CC(=O)N[CH]1[CH](O)[CH](O)[CH](C[CH](O)[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O)O[CH]1O[CH]4O[CH](CO)[CH](O)[CH](O)[CH]4NC(C)=O
CACTVS 3.385CC(C)CCCCCCCCC/C=C/C(=O)N[C@@H]1[C@@H](O)[C@@H](O)[C@@H](C[C@@H](O)[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O)O[C@H]1O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4NC(C)=O
OpenEye OEToolkits 2.0.6CC(C)CCCCCCCCCC=CC(=O)NC1C(C(C(OC1OC2C(C(C(C(O2)CO)O)O)NC(=O)C)CC(C3C(C(C(O3)N4C=CC(=O)NC4=O)O)O)O)O)O
OpenEye OEToolkits 2.0.6CC(C)CCCCCCCCC/C=C/C(=O)N[C@@H]1[C@H]([C@H]([C@H](O[C@H]1O[C@@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O)O)NC(=O)C)C[C@H]([C@@H]3[C@H]([C@H]([C@@H](O3)N4C=CC(=O)NC4=O)O)O)O)O)O
FormulaC38 H62 N4 O16
NameTunicamycin
ChEMBLCHEMBL4534172
DrugBank
ZINCZINC000096085312
PDB chain5o5e 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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PDB5o5e Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design.
Resolution3.4 Å
Binding residue
(original residue number in PDB)		Q44 L46 E56 W122 K125 L126 N182 N185 I186 A188 G189 I190 N191 F249 D252 R301 H302 R303 I304
Binding residue
(residue number reindexed from 1)		Q37 L39 E49 W104 K107 L108 N161 N164 I165 A167 G168 I169 N170 F228 D231 R280 H281 R282 I283
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.8.15: UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase.
Gene Ontology
Molecular Function
GO:0003975 UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity
GO:0003976 UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity
GO:0005515 protein binding
GO:0016757 glycosyltransferase activity
GO:0016780 phosphotransferase activity, for other substituted phosphate groups
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006047 UDP-N-acetylglucosamine metabolic process
GO:0006486 protein glycosylation
GO:0006487 protein N-linked glycosylation
GO:0006488 dolichol-linked oligosaccharide biosynthetic process
GO:0019348 dolichol metabolic process
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5o5e, PDBe:5o5e, PDBj:5o5e
PDBsum5o5e
PubMed30388443
UniProtQ9H3H5|GPT_HUMAN UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (Gene Name=DPAGT1)

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