Structure of PDB 2oi5 Chain A Binding Site BS01

Receptor Information
>2oi5 Chain A (length=449) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NAMSVVILAAGKGTRMYSDLPKVLHTLAGKAMVQHVIDAANELGAAHVHL
VYGHGGDLLKQALKDDNLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLY
GDVPLISVETLQRLRDAKPQGGIGLLTVKLDDPTGYGRITRENGKVTGIV
EHKDATDEQRQIQEINTGILIANGADMKRWLAKLTNNNAQGEYYITDIIA
LAYQEGREIVAVHPQRLSEVEGVNNRLQLSRLERVYQSEQAEKLLLAGVM
LRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGHRVKIGTGCVIKNSVI
GDDCEISPYTVVEDANLAAACTIGPFARLRPGAELLEGAHVGNFVEMKKA
RLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFV
GSDTQLVAPVTVGKGATIAAGTTVTRNVGENALAISRVPQTQKEGWRRP
Ligand information
Ligand IDACO
InChIInChI=1S/C23H38N7O17P3S/c1-12(31)51-7-6-25-14(32)4-5-26-21(35)18(34)23(2,3)9-44-50(41,42)47-49(39,40)43-8-13-17(46-48(36,37)38)16(33)22(45-13)30-11-29-15-19(24)27-10-28-20(15)30/h10-11,13,16-18,22,33-34H,4-9H2,1-3H3,(H,25,32)(H,26,35)(H,39,40)(H,41,42)(H2,24,27,28)(H2,36,37,38)/t13-,16-,17-,18+,22-/m1/s1
InChIKeyZSLZBFCDCINBPY-ZSJPKINUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
ACDLabs 10.04O=C(SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O)C
CACTVS 3.341CC(=O)SCCNC(=O)CCNC(=O)[CH](O)C(C)(C)CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0CC(=O)SCCNC(=O)CCNC(=O)C(C(C)(C)COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)O
FormulaC23 H38 N7 O17 P3 S
NameACETYL COENZYME *A
ChEMBLCHEMBL1230809
DrugBank
ZINCZINC000008551095
PDB chain2oi5 Chain A Residue 2000 [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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PDB2oi5 Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
Resolution2.25 Å
Binding residue
(original residue number in PDB)		G379 F402 G404 S405 A422 A423 R440
Binding residue
(residue number reindexed from 1)		G376 F399 G401 S402 A419 A420 R437
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) R18
Catalytic site (residue number reindexed from 1) R15
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:0005515 protein binding
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0016779 nucleotidyltransferase activity
GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity
GO:0042802 identical protein binding
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:0009245 lipid A biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2oi5, PDBe:2oi5, PDBj:2oi5
PDBsum2oi5
PubMed17473010
UniProtP0ACC7|GLMU_ECOLI Bifunctional protein GlmU (Gene Name=glmU)

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