Structure of PDB 1hm9 Chain B Binding Site BS04

Receptor Information
>1hm9 Chain B (length=458) Species: 1313 (Streptococcus pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SNFAIILAAGKGTRMKSDLPKVLHKVAGISMLEHVFRSVGAIQPEKTVTV
VGHKAELVEEVLAGQTEFVTQSEQLGTGHAVMMTEPILEGLSGHTLVIAG
DTPLITGESLKNLIDFHINHKNVATILTAETDNPFGYGRIVRNDNAEVLR
IVEQKDATDFEKQIKEINTGTYVFDNERLFEALKNINTNNAQGEYYITDV
IGIFRETGEKVGAYTLKDFDESLGVNDRVALATAESVMRRRINHKHMVNG
VSFVNPEATYIDIDVEIAPEVQIEANVILKGQTKIGAETVLTNGTYVVDS
TIGAGAVITNSMIEESSVADGVTVGPYAHIRPNSSLGAQVHIGNFVEVKG
SSIGENTKAGHLTYIGNCEVGSNVNFGAGTITVNYDGKNKYKTVIGDNVF
VGSNSTIIAPVELGDNSLVGAGSTITKDVPADAIAIGRGRQINKDEYATR
LPHHPKNQ
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 chain1hm9 Chain B Residue 2500 [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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PDB1hm9 Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
Resolution1.75 Å
Binding residue
(original residue number in PDB)		L8 A10 G11 Q72 Q75 G77 T78 Y138 G139 E154 N169 T170 Y197 T199 N227
Binding residue
(residue number reindexed from 1)		L7 A9 G10 Q71 Q74 G76 T77 Y137 G138 E153 N168 T169 Y196 T198 N226
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) R15
Catalytic site (residue number reindexed from 1) R14
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:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0000902 cell morphogenesis
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
GO:0008360 regulation of cell shape
GO:0009058 biosynthetic process
GO:0009245 lipid A biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization
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:1hm9, PDBe:1hm9, PDBj:1hm9
PDBsum1hm9
PubMed11118459
UniProtQ97R46|GLMU_STRPN Bifunctional protein GlmU (Gene Name=glmU)

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