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PDBsum entry 3ezo

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protein links
Transferase PDB id
3ezo

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
307 a.a. *
Waters ×346
* Residue conservation analysis
PDB id:
3ezo
Name: Transferase
Title: Crystal structure of acyl-carrier-protein s-malonyltransferase from burkholderia pseudomallei 1710b
Structure: Malonyl coa-acyl carrier protein transacylase. Chain: a. Engineered: yes
Source: Burkholderia pseudomallei 1710b. Organism_taxid: 320372. Strain: 1719b. Gene: burkholderia pseudomallei, burps1710b_2906, fabd. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.05Å     R-factor:   0.158     R-free:   0.208
Authors: Ssgcid,Seattle Structural Genomics Center For Infectious Disease (Ssgcid)
Key ref: L.Baugh et al. (2013). Combining functional and structural genomics to sample the essential Burkholderia structome. Plos One, 8, e53851. PubMed id: 23382856
Date:
23-Oct-08     Release date:   11-Nov-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q3JQ66  (Q3JQ66_BURP1) -  Malonyl CoA-acyl carrier protein transacylase from Burkholderia pseudomallei (strain 1710b)
Seq:
Struc:
310 a.a.
307 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.39  - [acyl-carrier-protein] S-malonyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA
holo-[ACP]
+ malonyl-CoA
= malonyl-[ACP]
+ CoA
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Plos One 8:e53851 (2013)
PubMed id: 23382856  
 
 
Combining functional and structural genomics to sample the essential Burkholderia structome.
L.Baugh, L.A.Gallagher, R.Patrapuvich, M.C.Clifton, A.S.Gardberg, T.E.Edwards, B.Armour, D.W.Begley, S.H.Dieterich, D.M.Dranow, J.Abendroth, J.W.Fairman, D.Fox, B.L.Staker, I.Phan, A.Gillespie, R.Choi, S.Nakazawa-Hewitt, M.T.Nguyen, A.Napuli, L.Barrett, G.W.Buchko, R.Stacy, P.J.Myler, L.J.Stewart, C.Manoil, W.C.Van Voorhis.
 
  ABSTRACT  
 
No abstract given.

 

 

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