Structure of PDB 7ns4 Chain b

Receptor sequence
>7ns4b (length=340) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
SELLDSFETEFAKFYTDSNLEETNLQKCLDHTHEFKSQLKKLKAHLNKHI
QESKPKRKRELIIEKLSKSQRQWDHSVKKQIKYVSQQSNRFNKSTLNKLK
EFDIDSVYVNKLPKETMENVNEAIGYHILRYSIDNMPLGNKNEAFQYLKD
VYGITNKESTEFIEMGQIVHDLKKGDTESCLKWCSNEMSNHTALSSLKFD
LYTLSAVNKELKECTSLFIKEYCAAKHIFFDSPLFLIVLSGLISFQFFIK
YKTIREWTTKDELPFDVKLPDFLTHFHPIFICPVLKEETTTENPPYSLAC
HHIISKKALDRLSKNGTITFKCCPVNTSMSSTKKVRFVML
3D structure
PDB7ns4 GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme.
Chainb
Resolution3.9 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 b H381 C401 C404 H302 C322 C323
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:7ns4, PDBe:7ns4, PDBj:7ns4
PDBsum7ns4
PubMed33905682
UniProtQ12508|RMD5_YEAST E3 ubiquitin-protein ligase RMD5 (Gene Name=RMD5)

[Back to BioLiP]