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Structure paper

TitleStructure-activity relationship of ipglycermide binding to phosphoglycerate mutases.
Journal, issue, pagesJ. Biol. Chem., Vol. 296, Page 100628-100628, Year 2021
Publish dateNov 4, 2020 (structure data deposition date)
AuthorsWiedmann, M. / Dranchak, P.K. / Aitha, M. / Queme, B. / Collmus, C.D. / Kashipathy, M.M. / Kanter, L. / Lamy, L. / Rogers, J.M. / Tao, D. ...Wiedmann, M. / Dranchak, P.K. / Aitha, M. / Queme, B. / Collmus, C.D. / Kashipathy, M.M. / Kanter, L. / Lamy, L. / Rogers, J.M. / Tao, D. / Battaile, K.P. / Rai, G. / Lovell, S. / Suga, H. / Inglese, J.
External linksJ. Biol. Chem. / PubMed:33812994
MethodsX-ray diffraction
Resolution1.8 - 2.1 Å
Structure data

PDB-7knf:
1.80A resolution structure of independent Phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (Ce-1 NHOH)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-7kng:
2.10A resolution structure of independent Phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (Ce-2 Y7F)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • caenorhabditis elegans (invertebrata)
KeywordsISOMERASE / phosphoglycerate mutase / ipglycermide / peptide inhibitors / metal ion binding

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