PDBsum entry 3ttw

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Oxidoreductase PDB id
Protein chains
726 a.a.
HEM ×4
Waters ×2834
PDB id:
Name: Oxidoreductase
Title: Structure of the f413e variant of e. Coli kate
Structure: Catalase hpii. Chain: a, b, c, d. Synonym: catalase kate, hydroxyperoxidase ii. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: b1732, jw1721, kate. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.62Å     R-factor:   0.159     R-free:   0.199
Authors: P.C.Loewen,V.Jha
Key ref: V.Jha et al. (2012). Mutation of Phe413 to Tyr in catalase KatE from Escherichia coli leads to side chain damage and main chain cleavage. Arch Biochem Biophys, 525, 207-214. PubMed id: 22172685
15-Sep-11     Release date:   12-Oct-11    
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Protein chains
Pfam   ArchSchema ?
P21179  (CATE_ECOLI) -  Catalase HPII
753 a.a.
726 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Catalase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 H2O2 = O2 + 2 H2O
2 × H(2)O(2)
= O(2)
+ 2 × H(2)O
      Cofactor: Heme; Mn(2+)
Bound ligand (Het Group name = HEM) matches with 95.45% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     oxidation-reduction process   5 terms 
  Biochemical function     oxidoreductase activity     7 terms  


Arch Biochem Biophys 525:207-214 (2012)
PubMed id: 22172685  
Mutation of Phe413 to Tyr in catalase KatE from Escherichia coli leads to side chain damage and main chain cleavage.
V.Jha, L.J.Donald, P.C.Loewen.
The monofunctional catalase KatE of Esherichia coli exhibits exceptional resistance to heat denaturation and proteolytic degradation. During an investigation of subtle conformation changes in Arg111 and Phe413 on the proximal side of the heme induced by H(2)O(2), variants at position R111, T115 and F413 were constructed. Because the residues are not situated in the distal side heme cavity where catalysis occurs, significant changes in reactivity were not expected and indeed, only small changes in the kinetic characteristics were observed in all of the variants. However, the F413Y variant was found to have undergone main chain cleavage whereas the R111A, T115A, F413E and F413K variants had not. Two sites of cleavage were identified in the crystal structure and by mass spectrometry at residues 111 and 115. In addition to main chain cleavage, modifications to the side chains of Tyr413, Thr115 and Arg111 were suggested by differences in the electron density maps compared to maps of the native and inactive variant H128N/F413Y. The inactive variant H128N/F413Y and the active variant T115A/F413Y both did not exhibit main chain cleavage and the R11A/F413Y variant exhibited less cleavage. In addition, the apparent modification of three side chains was largely absent in these variants. It is also significant that all three F413 single variants contained heme b suggesting that the fidelity of the phenyl group was important for mediating heme b oxidation to heme d. The reactions are attributed to the introduction of a new reactive center possibly involving a transient radical on Tyr413 formed during catalytic turn over.