Structure of PDB 4m2b Chain A Binding Site BS01

Receptor Information
>4m2b Chain A (length=483) Species: 5664 (Leishmania major) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KSLSAAAQACVKKMRDAKVNEACIRTFIAQHVMVSKGETGSIPDSAIMPV
DSLDALDSLTIECDNAVLQSTVVLKLNGGLGTGMGLCDAKTLLEVKDGKT
FLDFTALQVQYLRQHCSEHLRFMLMDSFNTSASTKSFLKARYPWLYQVFD
SEVELMQNQVPKILQDTLEPAAWAENPAYEWAPPGHGDIYTALYGSGKLQ
ELVEQGYRYMFVSNGDNLGATIDKRVLAYMEKEKIDFLMEVCRRTESDKK
GGHLARQTVYVKGKDGQPDAEKRVLDLRESAQCPKADMESFQDINKYSFF
NTNNLWIRLPVLLETMQEHGGTLPLPVIRNEKTVDSSNSASPKVYQLETA
MGAAIAMFESASAIVVPRSRFAPVKTCADLLALRSDAYVVTDDFRLVLDD
RCHGHPPVVDLDSAHYKMMNGFEKLVQHGVPSLVECKRVTVKGLVQFGAG
NVLTGTVTIENTDSASAFVIPDGAKLNDTTASP
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 chain4m2b Chain A Residue 1001 [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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PDB4m2b Catalytic Mechanism and Allosteric Regulation of Udp-Glucose Pyrophosphorylase from Leishmania Major
Resolution2.2 Å
Binding residue
(original residue number in PDB)		L81 G83 G84 Q162 G190 H191 N219 K255 G256 G257 E284 F305 N306 N308 F376 K380
Binding residue
(residue number reindexed from 1)		L76 G78 G79 Q157 G185 H186 N214 K250 G251 G252 E279 F300 N301 N303 F371 K375
Annotation score4
Enzymatic activity
Enzyme Commision number 2.7.7.9: UTP--glucose-1-phosphate uridylyltransferase.
Gene Ontology
Molecular Function
GO:0003983 UTP:glucose-1-phosphate uridylyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0070569 uridylyltransferase activity
Biological Process
GO:0005977 glycogen metabolic process
GO:0006011 UDP-glucose metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0031981 nuclear lumen
GO:0097014 ciliary plasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4m2b, PDBe:4m2b, PDBj:4m2b
PDBsum4m2b
PubMed
UniProtQ4QDU3

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