Structure of PDB 1i12 Chain A

Receptor sequence
>1i12A (length=154) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
LPDGFYIRRMEEGDLEQVTETLKVLTTVGTITPESFCKLIKYWNEATVWN
DKKIMQYNPMVIVDKRTETVAATGNIIIERKIIHELGLCGHIEDIAVNSK
YQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEM
QIRK
3D structure
PDB1i12 The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase.
ChainA
Resolution1.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.4: glucosamine-phosphate 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 ACO A V26 L27 I100 A101 Q107 G108 G110 G112 K113 D134 N139 F142 Y143 K145 V24 L25 I95 A96 Q102 G103 G105 G107 K108 D129 N134 F137 Y138 K140
Gene Ontology
Molecular Function
GO:0004343 glucosamine 6-phosphate N-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
Cellular Component
GO:0005634 nucleus
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:1i12, PDBe:1i12, PDBj:1i12
PDBsum1i12
PubMed11278591
UniProtP43577|GNA1_YEAST Glucosamine 6-phosphate N-acetyltransferase (Gene Name=GNA1)

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