3PGM: Phosphoglycerate mutase 1

The structure of yeast phosphoglycerate mutase at 0.28 nm resolution. Determined by X-ray diffraction at 2.8 Å resolution. Released 26 May 1982.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
3,708
Mol. weight
55.09 kDa
Ligands
3PG
Released
26 May 1982

Explore 3PGM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PGM contains 20 α-helices and 16 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and B: 10 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand4-521
β-strand712
α-helix14-174
α-helix29-4012
α-helix41-455
β-strand51-5551
α-helix58-7114
β-strand79-8131
α-helix99-1035
α-helix107-1115
α-helix154-1618
α-helix162-1665
α-helix167-1693
β-strand174-17631
α-helix182-1909
β-strand20512
β-strand209-21021
β-strand22411

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phosphoglycerate mutase 1A, Bprotein244Saccharomyces cerevisiaeP00950 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3PGM_1 Phosphoglycerate mutase 1 (chains A, B)
PKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKGVNVLVDYTSKLSRA
IQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAQTLKKFGEEKFNTYRRSFDVPP
PPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKLVGKTSMIAAHG
NSLRGLVKHLEGISDADIAKLNIPPGTILVFELDENLKPSKPSYYLDPEAAAAGAAAVAN
QGKK

Ligands and cofactors

IDNameFormulaCopies
3PG3-phosphoglyceric acidC3 H7 O7 P2

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structure and activity of phosphoglycerate mutase. Winn, S.I., Watson, H.C., Harkins, R.N. et al. Philos Trans R Soc London,ser B (1981) 293:121-130. PubMed

Other PDB entries of the same protein (UniProt P00950 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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