Structure of PDB 6om8 Chain J Binding Site BS02

Receptor Information
>6om8 Chain J (length=456) Species: 6239 (Caenorhabditis elegans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MTDQVFGKVSKVVCVGAGYVGGPTCAMIAHKCPHITVTVVDMNTAKIAEW
NSDKLPIYEPGLDEIVFAARGRNLFFSSDIPKAIAEADLIFISVNTPTDL
KYVESVSRTIAQYAGGPKIVVEKSTVPVKAAESIGCILREAQKNNLKFQV
LSNPEFLAEGTAMKDLANPDRVLIGGESSPEGLQAVAELVRIYENWVPRN
RIITTNTWSSELSKLVANAFLAQRISSINSISAVCEATGAEISEVAHAVG
YDTRIGSKFLQASVGFGGSCFQKDVLSLVYLCESLNLPQVADYWQGVINI
NNWQRRRFADKIIAELFNTVTDKKIAIFGFAFKKNTGDTRESSAIHVIKH
LMEEHAKLSVYDPKVQKSQMLNDLASVTSAQDVERLITVESDPYAAARGA
HAIVVLTEWDEFVELNYSQIHNDMQHPAAIFDGRLILDQKALREIGFRTF
AIGTSP
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 chain6om8 Chain J 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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PDB6om8 Conservation of Atypical Allostery inC. elegansUDP-Glucose Dehydrogenase.
Resolution2.449 Å
Binding residue
(original residue number in PDB)		T136 F169 L170 A171 K227 I238 F272 Q274 S276 F279 G280 C283 F284 F345 K346 R447
Binding residue
(residue number reindexed from 1)		T125 F156 L157 A158 K214 I225 F259 Q261 S263 F266 G267 C270 F271 F332 K333 R434
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) T136 E172 K227 N231 C283 D287
Catalytic site (residue number reindexed from 1) T125 E159 K214 N218 C270 D274
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:0002009 morphogenesis of an epithelium
GO:0006024 glycosaminoglycan biosynthetic process
GO:0006065 UDP-glucuronate biosynthetic process
GO:0009792 embryo development ending in birth or egg hatching
GO:0018991 egg-laying behavior
GO:0022414 reproductive process
GO:0040025 vulval development
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6om8, PDBe:6om8, PDBj:6om8
PDBsum6om8
PubMed31616809
UniProtQ19905|UGDH_CAEEL UDP-glucose 6-dehydrogenase (Gene Name=sqv-4)

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