Structure of PDB 4ygo Chain C

Receptor sequence
>4ygoC (length=170) Species: 243277 (Vibrio cholerae O1 biovar El Tor str. N16961) [Search protein sequence]
NSQLTLRALERGDLRFIHNLNNNRNIMSYWFEEPYESFDELEELYNKHIH
DNAERRFVVEDAQKNLIGLVELIEINYIHRSAEFQIIIAPEHQGKGFART
LINRALDYSFTILNLHKIYLHVAVENPKAVHLYEECGFVEEGHLVEEFFI
NGRYQDVKRMYILQSKYLNR
3D structure
PDB4ygo Substrate-Induced Allosteric Change in the Quaternary Structure of the Spermidine N-Acetyltransferase SpeG.
ChainC
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.57: diamine N-acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA C P35 E41 P34 E40
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004145 diamine N-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0046872 metal ion binding
Biological Process
GO:0006598 polyamine catabolic process
GO:0046203 spermidine catabolic process
GO:0046208 spermine catabolic 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:4ygo, PDBe:4ygo, PDBj:4ygo
PDBsum4ygo
PubMed26410587
UniProtQ9KL03|ATDA_VIBCH Spermidine N(1)-acetyltransferase (Gene Name=speG)

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