Structure of PDB 4edf Chain D Binding Site BS01

Receptor Information
>4edf Chain D (length=425) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLP
IYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISACARRIVQNSNGY
KIVTEKSTVPVRAAESIRRIFDANNLQVLSNPEFLAEGTAIKDLKNPDRV
LIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLA
QRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQ
KDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFKKIAI
LGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSDQ
VSRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFD
GRRVLDGLHNELQTIGFQIETIGKK
Ligand information
Ligand IDUPG
InChIInChI=1S/C15H24N2O17P2/c18-3-5-8(20)10(22)12(24)14(32-5)33-36(28,29)34-35(26,27)30-4-6-9(21)11(23)13(31-6)17-2-1-7(19)16-15(17)25/h1-2,5-6,8-14,18,20-24H,3-4H2,(H,26,27)(H,28,29)(H,16,19,25)/t5-,6-,8-,9-,10+,11-,12-,13-,14-/m1/s1
InChIKeyHSCJRCZFDFQWRP-JZMIEXBBSA-N
SMILES
SoftwareSMILES
CACTVS 3.370OC[C@H]1O[C@H](O[P](O)(=O)O[P](O)(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)N3C=CC(=O)NC3=O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 12.01O=C1C=CN(C(=O)N1)C2OC(C(O)C2O)COP(=O)(OP(=O)(OC3OC(C(O)C(O)C3O)CO)O)O
CACTVS 3.370OC[CH]1O[CH](O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C1=CN(C(=O)NC1=O)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@](=O)(O)O[P@](=O)(O)O[C@@H]3[C@@H]([C@H]([C@@H]([C@H](O3)CO)O)O)O)O)O
OpenEye OEToolkits 1.7.6C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OC3C(C(C(C(O3)CO)O)O)O)O)O
FormulaC15 H24 N2 O17 P2
NameURIDINE-5'-DIPHOSPHATE-GLUCOSE;
URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE ESTER
ChEMBLCHEMBL375951
DrugBankDB01861
ZINCZINC000008215472
PDB chain4edf Chain D Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4edf Cofactor binding triggers a molecular switch to allosterically activate human UDP-{alpha}-D-glucose 6-dehydrogenase.
Resolution2.08 Å
Binding residue
(original residue number in PDB)		E161 F162 L163 A164 E165 K220 I231 F265 K267 S269 F272 G273 C276 F277 F338 K339 R442
Binding residue
(residue number reindexed from 1)		E133 F134 L135 A136 E137 K192 I203 F237 K239 S241 F244 G245 C248 F249 F305 K306 R402
Annotation score4
Binding affinityMOAD: Kd=33uM
Enzymatic activity
Catalytic site (original residue number in PDB) T131 E165 K220 N224 C276 D280
Catalytic site (residue number reindexed from 1) T108 E137 K192 N196 C248 D252
Enzyme Commision number 1.1.1.22: UDP-glucose 6-dehydrogenase.
Gene Ontology
Molecular Function
GO:0003979 UDP-glucose 6-dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042802 identical protein binding
GO:0051287 NAD binding
Biological Process
GO:0001702 gastrulation with mouth forming second
GO:0006024 glycosaminoglycan biosynthetic process
GO:0006065 UDP-glucuronate biosynthetic process
GO:0015012 heparan sulfate proteoglycan biosynthetic process
GO:0030206 chondroitin sulfate biosynthetic process
GO:0034214 protein hexamerization
GO:0048666 neuron development
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4edf, PDBe:4edf, PDBj:4edf
PDBsum4edf
PubMed23106432
UniProtO60701|UGDH_HUMAN UDP-glucose 6-dehydrogenase (Gene Name=UGDH)

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