3G3Q: Eukaryotic polyphosphate polymerase

Crystal structure of a eukaryotic polyphosphate polymerase in complex with a phosphate polymer. Determined by X-ray diffraction at 2.64 Å resolution. Released 5 May 2009.

Method
X-ray diffraction
Resolution
2.64 Å
Organism
Saccharomyces cerevisiae
Chains
2
Atoms
4,939
Mol. weight
72.59 kDa
Ligands
PO4
Released
5 May 2009

Explore 3G3Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3G3Q contains 30 α-helices and 22 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: 15 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand194-203101
α-helix205-21814
α-helix2201
β-strand22111
α-helix2221
α-helix229-2302
α-helix232-2354
β-strand236-24381
α-helix248-2558
β-strand261-26881
β-strand275-28281
α-helix286-2883
β-strand293-30081
α-helix301-3033
α-helix304-3096
α-helix314-3229
α-helix329-34820
β-strand352-364131
β-strand372-384131
α-helix414-4163
β-strand417-41931
β-strand423-432101
α-helix439-4457
β-strand451-45221
α-helix458-4669
α-helix468-4703

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vacuolar transporter chaperone 4A, Bprotein295Saccharomyces cerevisiaeP47075 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3G3Q_1 Vacuolar transporter chaperone 4 (chains A, B)
GAMGKQQNFVRQTTKYWVHPDNITELKLIILKHLPVLVFNTNKEFEREDSAITSIYFDNE
NLDLYYGRLRKDEGAEAHRLRWYGGMSTDTIFVERKTHREDWTGEKSVKARFALKERHVN
DFLKGKYTVDQVFAKMRKEGKKPMNEIENLEALASEIQYVMLKKKLRPVVRSFYNRTAFQ
LPGDARVRISLDTELTMVREDNFDGVDRTHKNWRRTDIGVDWPFKQLDDKDICRFPYAVL
EVKLQTQLGQEPPEWVRELVGSHLVEPVPKFSKFIHGVATLLNDKVDSIPFWLPQ

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P29

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

Primary citation

Catalytic core of a membrane-associated eukaryotic polyphosphate polymerase. Hothorn, M., Neumann, H., Lenherr, E.D. et al. Science (2009) 324:513-516. DOI 10.1126/science.1168120 · PubMed

Other PDB entries of the same protein (UniProt P47075 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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