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PDBsum entry 5ful

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protein ligands metals links
Transferase PDB id
5ful

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
339 a.a.
Ligands
SAH
PG4
EDO ×2
Metals
_CA ×2
_CL
Waters ×309
PDB id:
5ful
Name: Transferase
Title: Crystal structure of mus musculus protein arginine methyltransferase 2 with sah
Structure: Protein arginine n-methyltransferase 2. Chain: a. Engineered: yes. Mutation: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf21.
Resolution:
1.89Å     R-factor:   0.167     R-free:   0.192
Authors: V.Cura,N.Troffer-Charlier,N.Marechal,L.Bonnefond,J.Cavarelli
Key ref: V.Cura et al. (2017). Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors. Febs J, 284, 77-96. PubMed id: 27879050 DOI: 10.1111/febs.13953
Date:
27-Jan-16     Release date:   09-Nov-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q3UKX1  (Q3UKX1_MOUSE) -  Protein arginine N-methyltransferase 2 from Mus musculus
Seq:
Struc:
445 a.a.
339 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.1.1.125  - Transferred entry: 2.1.1.319, 2.1.1.320, 2.1.1.321 and 2.1.1.322.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]
S-adenosyl-L-methionine
+ arginine-[histone]
=
S-adenosyl-L-homocysteine
Bound ligand (Het Group name = SAH)
corresponds exactly
+ N(omega)-methyl-arginine-[histone]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1111/febs.13953 Febs J 284:77-96 (2017)
PubMed id: 27879050  
 
 
Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.
V.Cura, N.Marechal, N.Troffer-Charlier, J.M.Strub, M.J.van Haren, N.I.Martin, S.Cianférani, L.Bonnefond, J.Cavarelli.
 
  ABSTRACT  
 
No abstract given.

 

 

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