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PDBsum entry 3pfh

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3pfh

 

 

 

 

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Contents
Protein chains
241 a.a. *
Ligands
SAH ×2
T3Q ×2
EDO
Waters ×478
* Residue conservation analysis
PDB id:
3pfh
Name: Transferase
Title: X-ray crystal structure the n,n-dimethyltransferase tylm1 from streptomyces fradiae in complex with sah and dtdp-quip3n
Structure: N-methyltransferase. Chain: a, d. Engineered: yes
Source: Streptomyces fradiae. Organism_taxid: 1906. Gene: tylm1, tylmi(orf3 ). Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.79Å     R-factor:   0.212     R-free:   0.266
Authors: A.E.Carney,H.M.Holden
Key ref: A.E.Carney and H.M.Holden (2011). Molecular architecture of TylM1 from Streptomyces fradiae: an N,N-dimethyltransferase involved in the production of dTDP-D-mycaminose. Biochemistry, 50, 780-787. PubMed id: 21142177
Date:
28-Oct-10     Release date:   15-Dec-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P95748  (TYLM1_STRFR) -  dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase from Streptomyces fradiae
Seq:
Struc:
255 a.a.
241 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.1.1.235  - dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: dTDP-3-amino-3,6-dideoxy-alpha-D-glucose + 2 S-adenosyl-L-methionine = dTDP-alpha-D-mycaminose + 2 S-adenosyl-L-homocysteine + 2 H+
dTDP-3-amino-3,6-dideoxy-alpha-D-glucose
+ 2 × S-adenosyl-L-methionine
= dTDP-alpha-D-mycaminose
+ 2 × S-adenosyl-L-homocysteine
+ 2 × H(+)
Bound ligand (Het Group name = SAH)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Biochemistry 50:780-787 (2011)
PubMed id: 21142177  
 
 
Molecular architecture of TylM1 from Streptomyces fradiae: an N,N-dimethyltransferase involved in the production of dTDP-D-mycaminose.
A.E.Carney, H.M.Holden.
 
  ABSTRACT  
 
No abstract given.

 

 

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