Structure of PDB 2o28 Chain A

Receptor sequence
>2o28A (length=182) Species: 9606 (Homo sapiens) [Search protein sequence]
PDETPMFDPSLLKEVDWSQNTATFSPAISPTHPGEGLVLRPLCTADLNRG
FFKVLGQLTETGVVSPEQFMKSFEHMKKSGDYYVTVVEDVTLGQIVATAT
LIIEHKFIHSCAKRGRVEDVVVSDECRGKQLGKLLLSTLTLLSKKLNCYK
ITLECLPQNVGFYKKFGYTVSEENYMCRRFLK
3D structure
PDB2o28 Crystal Structure of Glucosamine-Phosphate N-Acetyltransferase 1
ChainA
Resolution1.8 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 16G A T61 E120 D121 V122 R181 T59 E118 D119 V120 R179
BS02 COA A L60 V122 V123 V124 R129 G130 Q132 G134 K135 Q160 N161 F164 Y165 K167 L58 V120 V121 V122 R127 G128 Q130 G132 K133 Q158 N159 F162 Y163 K165
Gene Ontology
Molecular Function
GO:0004343 glucosamine 6-phosphate N-acetyltransferase activity
GO:0005515 protein binding
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0042802 identical protein binding
Biological Process
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
Cellular Component
GO:0000139 Golgi membrane
GO:0005768 endosome
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:0010008 endosome membrane
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2o28, PDBe:2o28, PDBj:2o28
PDBsum2o28
PubMed
UniProtQ96EK6|GNA1_HUMAN Glucosamine 6-phosphate N-acetyltransferase (Gene Name=GNPNAT1)

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