Structure of PDB 1x3w Chain A

Receptor sequence
>1x3wA (length=320) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
NNIDFDSIAKMLLIKYKDFILSKFKKAAPVENIRFQNLVHTNQFAQGVLG
QSQHLCTVYDNPSWHSIVLETLDLDLIYKNVDKEFAKDGHAEGENIYTDY
LVKELLRYFKQDFFKWCNKPDCNHCGQNTSENMTPLGSQGPNGEESKFNC
GTVEIYKCNRCGNITRFPRYNDPIKLLETRKGRCGEWCNLFTLILKSFGL
DVRYVWNREDHVWCEYFSNFLNRWVHVDSCEQSFDQPYIYSINWNKKMSY
CIAFGKDGVVDVSKRYILQNELPRDQIKEEDLKFLCQFITKRLRYSLNDD
EIYQLACRDEQEQIELIRGK
3D structure
PDB1x3w Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins.
ChainA
Resolution3.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.52: peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase.
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 FRU A E238 Q239 S240 Q243 E231 Q232 S233 Q236
BS02 GLC A Y177 N178 G192 E193 N196 Y170 N171 G185 E186 N189
BS03 ZN A C129 C132 C165 C168 C122 C125 C158 C161
Gene Ontology
Molecular Function
GO:0000224 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
GO:0036503 ERAD pathway
GO:0097466 ubiquitin-dependent glycoprotein ERAD pathway
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0120125 PNGase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1x3w, PDBe:1x3w, PDBj:1x3w
PDBsum1x3w
PubMed15964983
UniProtQ02890|PNG1_YEAST Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (Gene Name=PNG1)

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