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PDBsum entry 3ai9

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protein ligands metals links
Transferase PDB id
3ai9

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
211 a.a.
Ligands
SAM
Metals
_MG ×2
Waters ×174
PDB id:
3ai9
Name: Transferase
Title: Crystal structure of duf358 protein reveals a putative spout-class rrna methyltransferase
Structure: Upf0217 protein mj1640. Chain: x. Engineered: yes. Mutation: yes
Source: Methanocaldococcus jannaschii. Methanococcus jannaschii. Organism_taxid: 2190. Gene: mj1640. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.55Å     R-factor:   0.192     R-free:   0.237
Authors: Y.A.Yuan,H.Y.Chen
Key ref: H.Y.Chen and Y.A.Yuan (2010). Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase. J Mol Cell Biol, 2, 366-374. PubMed id: 21098051 DOI: 10.1093/jmcb/mjq034
Date:
11-May-10     Release date:   30-Mar-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q59034  (TRMY_METJA) -  tRNA (pseudouridine(54)-N(1))-methyltransferase from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Seq:
Struc:
205 a.a.
211 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.1.1.257  - tRNA (pseudouridine(54)-N(1))-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: pseudouridine54 in tRNA + S-adenosyl-L-methionine = N1- methylpseudouridine54 in tRNA + S-adenosyl-L-homocysteine + H+
pseudouridine(54) in tRNA
+ S-adenosyl-L-methionine
= N(1)- methylpseudouridine(54) in tRNA
+ S-adenosyl-L-homocysteine
+ H(+)
Bound ligand (Het Group name = SAM)
matches with 76.92% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1093/jmcb/mjq034 J Mol Cell Biol 2:366-374 (2010)
PubMed id: 21098051  
 
 
Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT-class RNA methyltransferase.
H.Y.Chen, Y.A.Yuan.
 
  ABSTRACT  
 
No abstract given.

 

 

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