PDBsum entry 1j3n

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Transferase PDB id
Protein chains
408 a.a. *
Waters ×462
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of 3-oxoacyl-(acyl-carrier protein) synthase ii from thermus thermophilus hb8
Structure: 3-oxoacyl-(acyl-carrier protein) synthase ii. Chain: a, b. Engineered: yes
Source: Thermus thermophilus. Organism_taxid: 274. Gene: fabf. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
2.00Å     R-factor:   0.210     R-free:   0.258
Authors: B.Bagautdinov,M.Miyano,T.H.Tahirov,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref: B.Bagautdinov et al. (2008). Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 358-366. PubMed id: 18453702
10-Feb-03     Release date:   11-Mar-03    
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Protein chains
Pfam   ArchSchema ?
Q5SL80  (Q5SL80_THET8) -  3-oxoacyl-[acyl-carrier-protein] synthase 2
408 a.a.
408 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     catalytic activity     5 terms  


Acta Crystallogr Sect F Struct Biol Cryst Commun 64:358-366 (2008)
PubMed id: 18453702  
Structure of 3-oxoacyl-(acyl-carrier protein) synthase II from Thermus thermophilus HB8.
B.Bagautdinov, Y.Ukita, M.Miyano, N.Kunishima.
The beta-ketoacyl-(acyl carrier protein) synthases (beta-keto-ACP synthases; KAS) catalyse the addition of two-carbon units to the growing acyl chain during the elongation phase of fatty-acid synthesis. As key regulators of bacterial fatty-acid synthesis, they are promising targets for the development of new antibacterial agents. The crystal structure of 3-oxoacyl-ACP synthase II from Thermus thermophilus HB8 (TtKAS II) has been solved by molecular replacement and refined at 2.0 A resolution. The crystal is orthorhombic, space group P2(1)2(1)2, with unit-cell parameters a = 72.07, b = 185.57, c = 62.52 A, and contains one homodimer in the asymmetric unit. The subunits adopt the well known alpha-beta-alpha-beta-alpha thiolase fold that is common to ACP synthases. The structural and sequence similarities of TtKAS II to KAS I and KAS II enzymes of known structure from other sources support the hypothesis of comparable enzymatic activity. The dimeric state of TtKAS II is important to create each fatty-acid-binding pocket. Closer examination of KAS structures reveals that compared with other KAS structures in the apo form, the active site of TtKAS II is more accessible because of the ;open' conformation of the Phe396 side chain.