Structure of PDB 1i12 Chain C

Receptor sequence
>1i12C (length=154) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SMSLPDGFYIRRMEEGDLEQVTETLKVLTTVGTITPESFCKLIKYWNEAT
VWNKIMQYNPMVIVDKRTETVAATGNIIIERKIIHELGLCGHIEDIAVNS
KYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVE
MQIR
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.
ChainC
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 C I100 Q107 G108 G110 G112 K113 D134 K138 N139 F142 Y143 K145 I96 Q103 G104 G106 G108 K109 D130 K134 N135 F138 Y139 K141
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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