Structure of PDB 8pmq Chain 2

Receptor sequence
>8pmq2 (length=355) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SELLDSFETEFAKFYTDSNLEETNLQKCLDHTHEFKSQLKKLKAHLNKHI
QESKKFKRKRELIIEKLSKSQRQWDHSVKKQIKYVSQQSNRFNKSTLNKL
KEFDIDSVYVNKLPKETMENVNEAIGYHILRYSIDNMPLGNKNEAFQYLK
DVYGITNKESTEFIEMGQIVHDLKKGDTESCLKWCSNEMESLSSNHTALS
SLKFDLYTLSAMSKVNKELKECTSLFIKEYCAAKHIFFDSPLFLIVLSGL
ISFQFFIKYKTIRELAHVDWTTKDELPFDVKLPDFLTHFHPIFICPVLKE
ETTTENPPYSLACHHIISKKALDRLSKNGTITFKCPYCPVNTSMSSTKKV
RFVML
3D structure
PDB8pmq Multisite phosphorylation dictates selective E2-E3 pairing as revealed by Ubc8/UBE2H-GID/CTLH assemblies.
Chain2
Resolution3.53 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.2.27: RING-type E3 ubiquitin transferase.
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 ZN 2 H381 C401 H315 C335
Gene Ontology
Molecular Function
GO:0004842 ubiquitin-protein transferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0061630 ubiquitin protein ligase activity
Biological Process
GO:0006511 ubiquitin-dependent protein catabolic process
GO:0016567 protein ubiquitination
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0045721 negative regulation of gluconeogenesis
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005777 peroxisome
GO:0005829 cytosol
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
PDBsum8pmq
PubMed38113892
UniProtQ12508|RMD5_YEAST E3 ubiquitin-protein ligase RMD5 (Gene Name=RMD5)

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