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Structure paper

TitleResolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 7233-7243, Year 2017
Publish dateDec 20, 2016 (structure data deposition date)
AuthorsChristensen, E.M. / Patel, S.M. / Korasick, D.A. / Campbell, A.C. / Krause, K.L. / Becker, D.F. / Tanner, J.J.
External linksJ. Biol. Chem. / PubMed:28258219
MethodsX-ray diffraction
Resolution1.85 - 1.92 Å
Structure data

PDB-5uat:
Structure of human PYCR-1 complexed with NADPH
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

PDB-5uau:
Structure of human PYCR-1 complexed with proline
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5uav:
Structure of human PYCR-1 complexed with NADPH and L-tetrahydrofuroic acid
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-5uaw:
Structure of apo human PYCR-1 crystallized in space group P21212
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-5uax:
Structure of apo human PYCR-1 crystallized in space group C2
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-PRO:
PROLINE

ChemComp-TFB:
TETRAHYDROFURAN-2-CARBOXYLIC ACID

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / AMINO-ACID BIOSYNTHESIS / PROLINE BIOSYNTHESIS

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