5B6B: Complex of LATS1 and phosphomimetic MOB1b
Complex of LATS1 and phosphomimetic MOB1b. Determined by X-ray diffraction at 3.54 Å resolution. Released 6 Jul 2016.
- Method
- X-ray diffraction
- Resolution
- 3.54 Å
- Organism
- Mus musculus
- Chains
- 16
- Atoms
- 16,626
- Mol. weight
- 286.24 kDa
- Ligands
- ZN
- Released
- 6 Jul 2016
Explore 5B6B in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5B6B contains 104 α-helices and 26 β-strands across 16 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: 11 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 41-45 | 5 | |
| α-helix | 47-48 | 2 | |
| α-helix | 53-74 | 22 | |
| β-strand | 88 | 1 | 1 |
| β-strand | 94 | 1 | 1 |
| β-strand | 97 | 1 | 2 |
| β-strand | 107 | 1 | 2 |
| α-helix | 111-126 | 16 | |
| α-helix | 138-141 | 4 | |
| α-helix | 144-164 | 21 | |
| α-helix | 168-172 | 5 | |
| α-helix | 176-193 | 18 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-204 | 3 | |
| α-helix | 205-211 | 7 | |
Chain B: 11 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 24-30 | 7 | |
| α-helix | 47-48 | 2 | |
| α-helix | 53-74 | 22 | |
| β-strand | 88 | 1 | 3 |
| β-strand | 94 | 1 | 3 |
| β-strand | 97 | 1 | 4 |
| β-strand | 107 | 1 | 4 |
| α-helix | 111-126 | 16 | |
| α-helix | 138-141 | 4 | |
| α-helix | 144-164 | 21 | |
| α-helix | 168-172 | 5 | |
| α-helix | 176-193 | 18 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-204 | 3 | |
| α-helix | 205-211 | 7 | |
Chains C, E, I and L: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 635-669 | 35 | |
| α-helix | 674-696 | 23 | |
Chain D: 11 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 26-30 | 5 | |
| α-helix | 47-48 | 2 | |
| α-helix | 53-74 | 22 | |
| β-strand | 88 | 1 | 5 |
| β-strand | 94 | 1 | 5 |
| α-helix | 111-126 | 16 | |
| α-helix | 138-141 | 4 | |
| α-helix | 144-164 | 21 | |
| α-helix | 168-172 | 5 | |
| α-helix | 176-193 | 18 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-204 | 3 | |
| α-helix | 205-211 | 7 | |
Chain F: 12 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-32 | 6 | |
| α-helix | 41-45 | 5 | |
| α-helix | 47-48 | 2 | |
| α-helix | 53-74 | 22 | |
| β-strand | 88 | 1 | 6 |
| β-strand | 94 | 1 | 6 |
| β-strand | 97 | 1 | 7 |
| β-strand | 107 | 1 | 7 |
| α-helix | 111-126 | 16 | |
| α-helix | 138-141 | 4 | |
| α-helix | 144-164 | 21 | |
| α-helix | 168-172 | 5 | |
| α-helix | 176-193 | 18 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-204 | 3 | |
| α-helix | 205-211 | 7 | |
Chain G: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 630-632 | 3 | |
| α-helix | 635-669 | 35 | |
| α-helix | 674-696 | 23 | |
Chain H: 12 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 24-31 | 8 | |
| α-helix | 40-44 | 5 | |
| α-helix | 47-48 | 2 | |
| α-helix | 53-74 | 22 | |
| β-strand | 88 | 1 | 8 |
| β-strand | 94 | 1 | 8 |
| β-strand | 97 | 1 | 9 |
| β-strand | 107 | 1 | 9 |
| α-helix | 111-126 | 16 | |
| α-helix | 138-141 | 4 | |
| α-helix | 144-164 | 21 | |
| α-helix | 168-172 | 5 | |
| α-helix | 176-193 | 18 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-204 | 3 | |
| α-helix | 205-211 | 7 | |
Chain J: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 635-670 | 36 | |
| α-helix | 674-696 | 23 | |
4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| MOB kinase activator 1B | A, B, D, F, H, K, M, O | protein | 218 | Mus musculus | Q8BPB0 (AlphaFold model) |
| Serine/threonine-protein kinase LATS1 | C, E, G, I, J, L, N, P | protein | 85 | Mus musculus | Q8BYR2 (AlphaFold model) |
Sequence of entity 1 (A, B, D, F, H, K, M, O), FASTA
>5B6B_1 MOB kinase activator 1B (chains A, B, D, F, H, K, M, O)
GPMSFLFGSRSSKDFKPKKNIPEGSHQYELLKHAEADLGSGNLRMAVMLPEGEDLNEWVA
VNTVDFFNQINMLYGTITDFCTEESCPVMSAGPKYEYHWADGTNIKKPIKCSAPKYIDYL
MTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDPVIQLQEEAH
LNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLTSKDR
Sequence of entity 2 (C, E, G, I, J, L, N, P), FASTA
>5B6B_2 Serine/threonine-protein kinase LATS1 (chains C, E, G, I, J, L, N, P)
GPKDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQD
QMRKMLCQKESNYIRLKRAKMDKSM
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 8 |
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:
- 5B5V 2.19 Å, Structure of full-length MOB1b
- 5B5W 2.96 Å, Crystal structure of MOB1-LATS1 NTR domain complex
Browse structure collections
About this viewer
MolViewer shows 5B6B directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.