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TitleStructural Evidence of Substrate Specificity in Mammalian Peroxidases: STRUCTURE OF THE THIOCYANATE COMPLEX WITH LACTOPEROXIDASE AND ITS INTERACTIONS AT 2.4 A RESOLUTION
Journal, issue, pagesJ. Biol. Chem., Vol. 284, Page 14849-14856, Year 2009
Publish dateOct 2, 2008 (structure data deposition date)
AuthorsSheikh, I.A. / Singh, A.K. / Singh, N. / Sinha, M. / Singh, S.B. / Bhushan, A. / Kaur, P. / Srinivasan, A. / Sharma, S. / Singh, T.P.
External linksJ. Biol. Chem. / PubMed:19339248
MethodsX-ray diffraction
Resolution2.4 - 2.7 Å
Structure data

PDB-3erh:
First structural evidence of substrate specificity in mammalian peroxidases: Crystal structures of substrate complexes with lactoperoxidases from two different species
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3eri:
First structural evidence of substrate specificity in mammalian peroxidases: Crystal structures of substrate complexes with lactoperoxidases from two different species
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3faq:
Crystal structure of lactoperoxidase complex with cyanide
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-SCN:
THIOCYANATE ION

ChemComp-CA:
Unknown entry

ChemComp-IOD:
IODIDE ION

ChemComp-HOH:
WATER

ChemComp-CYN:
CYANIDE ION

Source
  • bubalus bubalis (water buffalo)
  • bos taurus (cattle)
KeywordsOXIDOREDUCTASE / peroxidase / complex / heme / lactopeoxidase / Antibiotic / Antimicrobial / Cleavage on pair of basic residues / Glycoprotein / Hydrogen peroxide / Iron / Metal-binding / Secreted / Inhibitor

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