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Structure paper

TitleStructure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis.
Journal, issue, pagesBiochemistry, Vol. 40, Page 3900-3911, Year 2001
Publish dateJan 22, 2001 (structure data deposition date)
AuthorsWood, Z.A. / Poole, L.B. / Karplus, P.A.
External linksBiochemistry / PubMed:11300769
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-1hyu:
CRYSTAL STRUCTURE OF INTACT AHPF
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-HOH:
WATER

Source
  • salmonella typhimurium (bacteria)
KeywordsOXIDOREDUCTASE / Thiol-thiolate hydrogen bond / nucleotide binding fold / thioredoxin reductase / thioredoxin

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