Structure of PDB 3pjg Chain A Binding Site BS01

Receptor Information
>3pjg Chain A (length=389) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FMKITISGTGYVGLSNGVLIAQNHEVVALDIVQAKVDMLNQKISPIVDKE
IQEYLAEKPLNFRATTDKHDAYRNADYVIIATPTDYDPKTNYFNTSTVEA
VIRDVTEINPNAVMIIKSTIPVGFTRDIKERLGIDNVIFSPEFLREGRAL
YDNLHPSRIVIGERSARAERFADLLKEGAIKQDIPTLFTDSTEAEAIKLF
ANTYLALRVAYFNELDSYAESQGLNSKQIIEGVCLDPRIGNHYNNPSFGY
GGYCLPKDTKQLLANYESVPNNIIAAIVDANRTRKDFIADSILARKPKVV
GVYRLIMKSGSDNFRASSIQGIMKRIKAKGIPVIIYEPVMQEDEFFNSRV
VRDLNAFKQEADVIISNRMAEELADVADKVYTRDLFGND
Ligand information
Ligand IDUGA
InChIInChI=1S/C15H22N2O18P2/c18-5-1-2-17(15(26)16-5)12-9(22)6(19)4(32-12)3-31-36(27,28)35-37(29,30)34-14-10(23)7(20)8(21)11(33-14)13(24)25/h1-2,4,6-12,14,19-23H,3H2,(H,24,25)(H,27,28)(H,29,30)(H,16,18,26)/t4-,6-,7+,8+,9-,10-,11+,12-,14-/m1/s1
InChIKeyHDYANYHVCAPMJV-LXQIFKJMSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C3OC(OP(=O)(O)OP(=O)(O)OCC2OC(N1C(=O)NC(=O)C=C1)C(O)C2O)C(O)C(O)C3O
CACTVS 3.341O[CH]1[CH](O)[CH](O[CH]([CH]1O)C(O)=O)O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O
OpenEye OEToolkits 1.5.0C1=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)C(=O)O)O)O)O)O)O
CACTVS 3.341O[C@@H]1[C@@H](O)[C@H](O[C@@H]([C@H]1O)C(O)=O)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
OpenEye OEToolkits 1.5.0C1=CN(C(=O)NC1=O)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OC3C(C(C(C(O3)C(=O)O)O)O)O)O)O
FormulaC15 H22 N2 O18 P2
NameURIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID;
UDP-GLUCURONIC ACID
ChEMBLCHEMBL228057
DrugBankDB03041
ZINCZINC000008215691
PDB chain3pjg Chain A Residue 901 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3pjg Conformational change upon product binding to Klebsiella pneumoniae UDP-glucose dehydrogenase: a possible inhibition mechanism for the key enzyme in polymyxin resistance.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		F142 L143 R144 K197 N201 V208 Y242 N244 S246 Y249 G250 Y252 M306 D388
Binding residue
(residue number reindexed from 1)		F143 L144 R145 K198 N202 V209 Y243 N245 S247 Y250 G251 Y253 M307 D389
Annotation score4
Binding affinityPDBbind-CN: -logKd/Ki=3.55,Ki=283uM
Enzymatic activity
Catalytic site (original residue number in PDB) T118 E145 K197 N201 C253 D257
Catalytic site (residue number reindexed from 1) T119 E146 K198 N202 C254 D258
Enzyme Commision number 1.1.1.22: UDP-glucose 6-dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0051287 NAD binding
Biological Process
GO:0000271 polysaccharide biosynthetic process
GO:0006065 UDP-glucuronate biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3pjg, PDBe:3pjg, PDBj:3pjg
PDBsum3pjg
PubMed21536136
UniProtA0A0J9WZA6

[Back to BioLiP]