Structure of PDB 1fwy Chain B Binding Site BS01

Receptor Information
>1fwy Chain B (length=324) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NNAMSVVILAAGKGTRMYSDLPKVLHTLAGKAMVQHVIDAANELGAAHVH
LVYGHGGDLLKQALKDDNLNWVLQAEQLGTGHAMQQAAPFFADDEDILML
YGDVPLISVETLQRLRDAKPQGGIGLLTVKLDDPTGYGRITRENGKVTGI
VEHKDATDEQRQIQEINTGILIANGADMKRWLAKLTNNNAQGEYYITDII
ALAYQEGREIVAVHPQRLSEVEGVNNRLQLSRLERVYQSEQAEKLLLAGV
MLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGHRVKIGTGCVIKNSV
IGDDCEISPYTVVEDANLAAACTI
Ligand information
Ligand IDUD1
InChIInChI=1S/C17H27N3O17P2/c1-6(22)18-10-13(26)11(24)7(4-21)35-16(10)36-39(31,32)37-38(29,30)33-5-8-12(25)14(27)15(34-8)20-3-2-9(23)19-17(20)28/h2-3,7-8,10-16,21,24-27H,4-5H2,1H3,(H,18,22)(H,29,30)(H,31,32)(H,19,23,28)/t7-,8-,10-,11-,12-,13-,14-,15-,16-/m1/s1
InChIKeyLFTYTUAZOPRMMI-CFRASDGPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)NC1C(C(C(OC1OP(=O)(O)OP(=O)(O)OCC2C(C(C(O2)N3C=CC(=O)NC3=O)O)O)CO)O)O
CACTVS 3.341CC(=O)N[CH]1[CH](O)[CH](O)[CH](CO)O[CH]1O[P](O)(=O)O[P](O)(=O)OC[CH]2O[CH]([CH](O)[CH]2O)N3C=CC(=O)NC3=O
ACDLabs 10.04O=P(OC1OC(C(O)C(O)C1NC(=O)C)CO)(O)OP(=O)(O)OCC3OC(N2C=CC(=O)NC2=O)C(O)C3O
CACTVS 3.341CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[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 1.5.0CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[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)CO)O)O
FormulaC17 H27 N3 O17 P2
NameURIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
ChEMBLCHEMBL388154
DrugBankDB03397
ZINCZINC000008551100
PDB chain1fwy Chain B Residue 502 [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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PDB1fwy Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		L11 A13 G14 Q76 Q79 G81 T82 Y103 D105 Y139 G140 E154 N169 Y197 T199
Binding residue
(residue number reindexed from 1)		L9 A11 G12 Q74 Q77 G79 T80 Y101 D103 Y137 G138 E152 N167 Y195 T197
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) R18
Catalytic site (residue number reindexed from 1) R16
Enzyme Commision number 2.3.1.157: glucosamine-1-phosphate N-acetyltransferase.
2.7.7.23: UDP-N-acetylglucosamine diphosphorylase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity
GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity
Biological Process
GO:0000902 cell morphogenesis
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fwy, PDBe:1fwy, PDBj:1fwy
PDBsum1fwy
PubMed10428949
UniProtP0ACC7|GLMU_ECOLI Bifunctional protein GlmU (Gene Name=glmU)

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