Molecular Target Synopsis
Overview
Domains and Structures
Drugs and Clinical Candidates
Druggability
Chemistry
Ligand Efficiency Plot
Pathways
Family Cladogram
Interaction Network
Gene Expression
Gene Copy Number Variation
RNAi
Mutations
Germline Genetics

fusA (Q5SHN5) - Overview - Molecular Target Synopsis

Protein


fusA, Elongation factor G
UniProt Q5SHN5

Also Known as EFG_THET8, fusA, fus

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

2OM7
STRUCTURAL BASIS FOR INTERACTION OF THE RIBOSOME WITH THE SWITCH REGIONS OF GTP-BOUND ELONGATION FACTORS
RCSB/PDB
Inspect Structure
See all 3D Structures for fusA

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform
691Q5SHN5-1, P13551-1

Sub-cellular localization


UniProt: fusA is active in the following subcellular-locations: cytoplasm.
GO terms: fusA is active in the following subcellular-locations: cytoplasm.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project fusA has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For fusA there are:
5 structures (5 chains) solved
3 are solved in complex with at least one small molecule ligand



(see details)
Molecular Target 3D Synopsis

Screening and Chemistry


fusA has been screened with compounds ( bioactivities). (see details)