Structure of PDB 3prj Chain B Binding Site BS02

Receptor Information
>3prj Chain B (length=459) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTL
PIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGK
GRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKP
NLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYE
HWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEE
VATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYW
QQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSS
IYISKYLMDEGAHLHIYDPKVPREQIVVDLSDQVSRLVTISKDPYEACDG
AHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGF
QIETIGKKV
Ligand information
Ligand IDUDX
InChIInChI=1S/C14H22N2O16P2/c17-5-3-28-13(11(22)8(5)19)31-34(26,27)32-33(24,25)29-4-6-9(20)10(21)12(30-6)16-2-1-7(18)15-14(16)23/h1-2,5-6,8-13,17,19-22H,3-4H2,(H,24,25)(H,26,27)(H,15,18,23)/t5-,6-,8+,9-,10-,11-,12-,13-/m1/s1
InChIKeyDQQDLYVHOTZLOR-OCIMBMBZSA-N
SMILES
SoftwareSMILES
CACTVS 3.341O[C@@H]1CO[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]1O
ACDLabs 10.04O=P(OC1OCC(O)C(O)C1O)(O)OP(=O)(O)OCC3OC(N2C=CC(=O)NC2=O)C(O)C3O
OpenEye OEToolkits 1.5.0C1C(C(C(C(O1)OP(=O)(O)OP(=O)(O)OCC2C(C(C(O2)N3C=CC(=O)NC3=O)O)O)O)O)O
OpenEye OEToolkits 1.5.0C1[C@H]([C@@H]([C@H]([C@H](O1)O[P@](=O)(O)O[P@](=O)(O)OC[C@@H]2[C@H]([C@H]([C@@H](O2)N3C=CC(=O)NC3=O)O)O)O)O)O
CACTVS 3.341O[CH]1CO[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]1O
FormulaC14 H22 N2 O16 P2
NameURIDINE-5'-DIPHOSPHATE-XYLOPYRANOSE;
UDP-ALPHA-D-XYLOPYRANOSE
ChEMBL
DrugBankDB01713
ZINCZINC000008551129
PDB chain3prj Chain B 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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PDB3prj Role of Packing Defects in the Evolution of Allostery and Induced Fit in Human UDP-Glucose Dehydrogenase.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		T131 F162 L163 A164 E165 K220 I231 F265 K267 S269 F272 C276 F277 F338 K339 R442
Binding residue
(residue number reindexed from 1)		T131 F162 L163 A164 E165 K220 I231 F265 K267 S269 F272 C276 F277 F338 K339 R435
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) T131 E165 K220 N224 C276 D280
Catalytic site (residue number reindexed from 1) T131 E165 K220 N224 C276 D280
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:3prj, PDBe:3prj, PDBj:3prj
PDBsum3prj
PubMed21595445
UniProtO60701|UGDH_HUMAN UDP-glucose 6-dehydrogenase (Gene Name=UGDH)

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