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Structure paper

TitleSerine Hydroxymethyltransferase: Role of Glu75 and Evidence that Serine Is Cleaved by a Retroaldol Mechanism.
Journal, issue, pagesBiochemistry, Vol. 43, Page 6865-6876, Year 2004
Publish dateDec 12, 2003 (structure data deposition date)
AuthorsSzebenyi, D.M. / Musayev, F.N. / di Salvo, M.L. / Safo, M.K. / Schirch, V.
External linksBiochemistry / PubMed:15170323
MethodsX-ray diffraction
Resolution2.4 - 2.95 Å
Structure data

PDB-1rv3:
E75L MUTANT OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE, COMPLEX WITH GLYCINE
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1rv4:
E75L MUTANT OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-1rvu:
E75Q MUTANT OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1rvy:
E75Q MUTANT OF RABBIT CYTOSOLIC SERINE HYDROXYMETHYLTRANSFERASE, COMPLEX WITH GLYCINE
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-GLY:
GLYCINE

ChemComp-HOH:
WATER

ChemComp-PLG:
N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]

Source
  • oryctolagus cuniculus (rabbit)
KeywordsTRANSFERASE / ONE-CARBON METABOLISM / ONE CARBON METABOLISM / HYDROLASE

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