5B5V: Full-length MOB1b

Structure of full-length MOB1b. Determined by X-ray diffraction at 2.19 Å resolution. Released 6 Jul 2016.

Method
X-ray diffraction
Resolution
2.19 Å
Organism
Mus musculus
Chains
6
Atoms
6,325
Mol. weight
151.99 kDa
Ligands
ZN
Released
6 Jul 2016

Explore 5B5V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5B5V contains 49 α-helices and 12 β-strands across 6 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 C: 11 helices, 3 β-strands

ElementResiduesLengthSheet
α-helix24-3411
α-helix35-384
α-helix41-444
α-helix53-7422
β-strand87-8821
β-strand94-9851
β-strand10711
α-helix111-12616
α-helix139-1413
α-helix144-17330
α-helix176-19318
α-helix198-2014
α-helix202-2043
α-helix205-2095
Chain B: 14 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix24-3512
α-helix36-383
α-helix41-444
α-helix47-482
α-helix53-7422
α-helix76-783
β-strand87-8822
β-strand94-9522
α-helix111-12616
α-helix139-1413
α-helix144-16522
α-helix167-1726
α-helix176-19217
α-helix198-2014
α-helix202-2043
α-helix205-2117
Chain D: 13 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix24-3512
α-helix36-383
α-helix41-444
α-helix47-482
α-helix53-7422
α-helix76-783
β-strand87-8824
β-strand94-9524
α-helix111-12616
α-helix139-1413
α-helix144-16522
α-helix167-1726
α-helix176-19217
α-helix202-2043
α-helix205-2095
Chains E and F: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand5-951

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MOB kinase activator 1BA, B, C, D, E, Fprotein218Mus musculusQ8BPB0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>5B5V_1 MOB kinase activator 1B (chains A, B, C, D, E, F)
GPMSFLFGSRSSKTFKPKKNIPEGSHQYELLKHAEATLGSGNLRMAVMLPEGEDLNEWVA
VNTVDFFNQINMLYGTITDFCTEESCPVMSAGPKYEYHWADGTNIKKPIKCSAPKYIDYL
MTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDPVIQLQEEAH
LNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLTSKDR

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

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

Primary citation

Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway. Kim, S.Y., Tachioka, Y., Mori, T. et al. Sci Rep (2016) 6:28488-28488. DOI 10.1038/srep28488 · PubMed

Other PDB entries of the same protein (UniProt Q8BPB0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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