Structure of PDB 1i12 Chain D

Receptor sequence
>1i12D (length=157) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SMSLPDGFYIRRMEEGDLEQVTETLKVLTTVGTITPESFCKLIKYWNEAT
VWNDNKIMQYNPMVIVDKRTETVAATGNIIIERKIIHELGLCGHIEDIAV
NSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAG
VEMQIRK
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.
ChainD
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 D I100 A101 V102 Q107 G108 Q109 G110 G112 K113 D134 K138 F142 Y143 K145 I98 A99 V100 Q105 G106 Q107 G108 G110 K111 D132 K136 F140 Y141 K143
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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