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TitleA Hotspot for Disease-Associated Variants of Human PGM1 Is Associated with Impaired Ligand Binding and Loop Dynamics.
Journal, issue, pagesStructure, Vol. 26, Page 1337-, Year 2018
Publish dateMar 29, 2017 (structure data deposition date)
AuthorsStiers, K.M. / Beamer, L.J.
External linksStructure / PubMed:30122451
MethodsX-ray diffraction
Resolution1.75000083769 - 2.60004291837 Å
Structure data

PDB-5vbi:
Crystal Structure of the R515W missense variant of human PGM1
Method: X-RAY DIFFRACTION / Resolution: 1.75000083769 Å

PDB-5vec:
Crystal Structure of the R515L missense variant of human PGM1
Method: X-RAY DIFFRACTION / Resolution: 2.20001616144 Å

PDB-5vg7:
Crystal Structure of the R503Q missense variant of human PGM1
Method: X-RAY DIFFRACTION / Resolution: 1.95000322932 Å

PDB-5vin:
Crystal Structure of the R515Q missense variant of human PGM1
Method: X-RAY DIFFRACTION / Resolution: 2.60004291837 Å

PDB-6uiq:
Crystal structure of wild-type human phosphoglucomutase 1 in complex with Glucose-6-Phosphate
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-CO:
Unknown entry

ChemComp-G6P:
6-O-phosphono-alpha-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsISOMERASE / phosphoglucomutase-1 / PGM1 / phosphoryl transfer / phosphoglucomutase / G6P

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