Structure of PDB 1hv9 Chain B Binding Site BS01

Receptor Information
>1hv9 Chain B (length=450) 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
IGDDCEISPYTVVEDANLAAACTIGPFARLRPGAELLEGAHVGNFVEMKK
ARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVF
VGSDTQLVAPVTVGKGATIAAGTTVTRNVGENALAISRVPQTQKEGWRRP
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain1hv9 Chain B Residue 9027 [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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PDB1hv9 Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		D105 N227
Binding residue
(residue number reindexed from 1)		D103 N225
Annotation score1
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: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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1hv9, PDBe:1hv9, PDBj:1hv9
PDBsum1hv9
PubMed11329257
UniProtP0ACC7|GLMU_ECOLI Bifunctional protein GlmU (Gene Name=glmU)

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