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TitleBacillus anthracis Prolyl 4-Hydroxylase Modifies Collagen-like Substrates in Asymmetric Patterns.
Journal, issue, pagesJ. Biol. Chem., Vol. 291, Page 13360-13374, Year 2016
Publish dateFeb 21, 2016 (structure data deposition date)
AuthorsSchnicker, N.J. / Dey, M.
External linksJ. Biol. Chem. / PubMed:27129244
MethodsX-ray diffraction
Resolution1.67 - 2.1 Å
Structure data

PDB-5iat:
Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual Bacterial Prolyl Hydroxylase - apo-BaP4H
Method: X-RAY DIFFRACTION / Resolution: 1.67 Å

PDB-5iav:
Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual Bacterial Prolyl Hydroxylase - Co-BaP4H-MLI
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-5iax:
Mechanistic and Structural Analysis of Substrate Recognition and Cofactor Binding by an Unusual Bacterial Prolyl Hydroxylase - Co-BaP4H-PPG
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-CO:
Unknown entry

ChemComp-MLI:
MALONATE ION

ChemComp-AKG:
2-OXOGLUTARIC ACID

ChemComp-BME:
BETA-MERCAPTOETHANOL

Source
  • bacillus anthracis (anthrax bacterium)
KeywordsOXIDOREDUCTASE / P4H / Dioxygenase / Cupin / Fe(II)/alpha-ketoglutarate

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