2VPV: Dimerization Domain of Mif2p

Dimerization Domain of Mif2p. Determined by X-ray diffraction at 2.7 Å resolution. Released 26 Aug 2008.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
SACCHAROMYCES CEREVISIAE
Chains
2
Atoms
1,519
Mol. weight
37.54 kDa
Released
26 Aug 2008

Explore 2VPV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VPV contains 3 α-helices and 19 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.

Chain A: 2 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand43811
β-strand443-44422
β-strand453-45972
α-helix463-4653
β-strand467-47041
β-strand474-48292
β-strand484-48961
β-strand492-49761
β-strand501-50442
β-strand509-51461
α-helix5191
β-strand520-52892
Chain B: 1 helix, 9 β-strands
ElementResiduesLengthSheet
β-strand440-44453
β-strand453-45973
β-strand466-46834
β-strand474-48293
β-strand484-48964
β-strand492-49764
β-strand501-50443
β-strand510-51454
α-helix5191
β-strand520-52893

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein MIF2A, Bprotein166SACCHAROMYCES CEREVISIAEP35201 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2VPV_1 PROTEIN MIF2 (chains A, B)
DPNAKENLIPEDPNEDIIERIESGGIENGEWLKHGILEANVKISDTKEETKDEIIAFAPN
LSQTEQVKDTKDENFALEIMFDKHKEYFASGILKLPAISGQKKLSNSFRTYITFHVIQGI
VEVTVCKNKFLSVKGSTFQIPAFNEYAIANRGNDEAKMFFVQVTVS

Primary citation

Structural and Functional Dissection of Mif2P, a Conserved DNA-Binding Kinetochore Protein. Cohen, R.L., Espelin, C.W., De Wulf, P. et al. Mol Biol Cell (2008) 19:4480. DOI 10.1091/MBC.E08-03-0297 · PubMed

Other PDB entries of the same protein (UniProt P35201 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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