Structure of PDB 1x3z Chain A Binding Site BS05
Receptor Information
>1x3z Chain A (length=320) Species:
4932
(Saccharomyces cerevisiae) [
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NNIDFDSIAKMLLIKYKDFILSKFKKAAPVENIRFQNLVHTNQFAQGVLG
QSQHLCTVYDNPSWHSIVLETLDLDLIYKNVDKEFAKDGHAEGENIYTDY
LVKELLRYFKQDFFKWCNKPDCNHCGQNTSENMTPLGSQGPNGEESKFNC
GTVEIYKCNRCGNITRFPRYNDPIKLLETRKGRCGEWCNLFTLILKSFGL
DVRYVWNREDHVWCEYFSNFLNRWVHVDSCEQSFDQPYIYSINWNKKMSY
CIAFGKDGVVDVSKRYILQNELPRDQIKEEDLKFLCQFITKRLRYSLNDD
EIYQLACRDEQEQIELIRGK
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1x3z Chain A Residue 999 [
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Receptor-Ligand Complex Structure
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PDB
1x3z
Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
C129 C132 C165 C168
Binding residue
(residue number reindexed from 1)
C122 C125 C158 C161
Annotation score
4
Enzymatic activity
Enzyme Commision number
3.5.1.52
: peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase.
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1x3z
,
PDBe:1x3z
,
PDBj:1x3z
PDBsum
1x3z
PubMed
15964983
UniProt
Q02890
|PNG1_YEAST Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (Gene Name=PNG1)
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