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Structure paper

TitleStructure and function of a novel LD-carboxypeptidase a involved in peptidoglycan recycling.
Journal, issue, pagesJ. Bacteriol., Vol. 195, Page 5555-5566, Year 2013
Publish dateJan 30, 2009 (structure data deposition date)
AuthorsDas, D. / Herve, M. / Elsliger, M.A. / Kadam, R.U. / Grant, J.C. / Chiu, H.J. / Knuth, M.W. / Klock, H.E. / Miller, M.D. / Godzik, A. ...Das, D. / Herve, M. / Elsliger, M.A. / Kadam, R.U. / Grant, J.C. / Chiu, H.J. / Knuth, M.W. / Klock, H.E. / Miller, M.D. / Godzik, A. / Lesley, S.A. / Deacon, A.M. / Mengin-Lecreulx, D. / Wilson, I.A.
External linksJ. Bacteriol. / PubMed:24123814
MethodsX-ray diffraction
Resolution1.89 Å
Structure data

PDB-3g23:
Crystal structure of a ld-carboxypeptidase a (saro_1426) from novosphingobium aromaticivorans dsm at 1.89 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL


ChemComp, No image

ChemComp-UNL:
Unknown ligand

ChemComp-HOH:
WATER

Source
  • novosphingobium aromaticivorans (bacteria)
KeywordsHYDROLASE / Flavodoxin-like fold / catalytic triad / merops s66 unassigned peptidases family / the swivelling beta/beta/alpha domain fold / structural genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-2

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