Structure of PDB 8pmq Chain 9 Binding Site BS01
Receptor Information
>8pmq Chain 9 (length=412) Species:
4932
(Saccharomyces cerevisiae) [
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KSIFNEPDVDFHLKLNQQLFHIPYELLSKRIKHTQAVINKETKSLHEHTA
ALNQIFEHNDVEHDELALAKITEMIRKVDHIERFLNTQIKSYCQILNRIK
KRLEFFHELKDIKSQNEGTRTKLIQWYQSYTNILIGDYLTRNNPIKYNSE
TKDHWNSGVVFLKQSQLDDLIDYDVLLEANRISTSLLHERNLLPLISWIN
ENKKTLTKKSSILEFQARLQEYIELLKVDNYTDAIVCFQRFLLPFVKSNF
TDLKLASGLLIFFERYLNLLDDQRWSVLNDLFLSDFYSMYGISQNDPLLI
YLSLGISSLKTRDCLHLQLFTLHSLKRKNCPVCSETFKPITQALPFAHHI
QSQLFENPILLPNGNVYDSKKLKKLAKTLKKQNLISLNPGQIMDPVDMKI
FCESDSIKMYPT
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
8pmq Chain 9 Residue 601 [
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Receptor-Ligand Complex Structure
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PDB
8pmq
Multisite phosphorylation dictates selective E2-E3 pairing as revealed by Ubc8/UBE2H-GID/CTLH assemblies.
Resolution
3.53 Å
Binding residue
(original residue number in PDB)
C395 C434
Binding residue
(residue number reindexed from 1)
C314 C330
Annotation score
4
Enzymatic activity
Enzyme Commision number
2.3.2.27
: RING-type E3 ubiquitin transferase.
Gene Ontology
Molecular Function
GO:0004842
ubiquitin-protein transferase activity
GO:0005515
protein binding
GO:0016740
transferase activity
GO:0046872
metal ion binding
GO:0061630
ubiquitin protein ligase activity
Biological Process
GO:0016567
protein ubiquitination
GO:0043066
negative regulation of apoptotic process
GO:0043161
proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0045721
negative regulation of gluconeogenesis
Cellular Component
GO:0005634
nucleus
GO:0005737
cytoplasm
GO:0034657
GID complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:8pmq
,
PDBe:8pmq
,
PDBj:8pmq
PDBsum
8pmq
PubMed
38113892
UniProt
P40492
|FYV10_YEAST Protein FYV10 (Gene Name=FYV10)
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