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PDBsum entry 3om2

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protein ligands metals links
Transferase PDB id
3om2

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
448 a.a.
Ligands
CIT ×2
Metals
_MG ×2
_CA
Waters ×657
PDB id:
3om2
Name: Transferase
Title: Crystal structure of b. Megaterium levansucrase mutant d257a
Structure: Levansucrase. Chain: a. Fragment: levansucrase sacb, unp residues 29-484. Engineered: yes. Mutation: yes
Source: Bacillus megaterium. Bacillus fructosus. Organism_taxid: 1404. Gene: sacb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.163     R-free:   0.218
Authors: C.P.Strube,A.Homann,M.Gamer,D.Jahn,J.Seibel,D.W.Heinz
Key ref: C.P.Strube et al. (2011). Polysaccharide synthesis of the levansucrase SacB from Bacillus megaterium is controlled by distinct surface motifs. J Biol Chem, 286, 17593-17600. PubMed id: 21454585
Date:
26-Aug-10     Release date:   23-Mar-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
D5DC07  (D5DC07_PRIM3) -  Levansucrase from Priestia megaterium (strain DSM 319 / IMG 1521)
Seq:
Struc:
484 a.a.
448 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.2.4.1.10  - levansucrase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: [6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose
[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside
+ sucrose
= [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside
+
D-glucose
Bound ligand (Het Group name = CIT)
matches with 47.06% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
J Biol Chem 286:17593-17600 (2011)
PubMed id: 21454585  
 
 
Polysaccharide synthesis of the levansucrase SacB from Bacillus megaterium is controlled by distinct surface motifs.
C.P.Strube, A.Homann, M.Gamer, D.Jahn, J.Seibel, D.W.Heinz.
 
  ABSTRACT  
 
No abstract given.

 

 

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