5BRM: MOB kinase activator 1A

Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signaling. Determined by X-ray diffraction at 2.65 Å resolution. Released 8 Jul 2015.

Method: X-ray diffraction
Resolution: 2.65 Å
Organism: Homo sapiens
Chains: 15
Atoms: 8,912
Mol. weight: 158.75 kDa
Ligands: ZN
Released: 8 Jul 2015

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

Secondary structure: helices and β-sheets

5BRM contains 56 α-helices and 29 β-strands across 15 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: 7 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	53-73	21
α-helix	76-78	3
β-strand	87-88	2	1
β-strand	93-95	3	1
β-strand	97	1	2
β-strand	107	1	2
α-helix	111-126	16
α-helix	144-172	29
α-helix	176-192	17
α-helix	202-204	3
α-helix	205-210	6

Chain B: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	53-73	21
α-helix	76-78	3
β-strand	87-88	2	3
β-strand	93-95	3	3
β-strand	97	1	4
β-strand	107	1	4
α-helix	111-126	16
α-helix	139-141	3
α-helix	144-165	22
α-helix	167-172	6
α-helix	176-193	18
α-helix	202-204	3
α-helix	205-210	6

Chain C: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	53-73	21
α-helix	76-78	3
β-strand	88	1	5
β-strand	94-95	2	5
β-strand	97	1	6
β-strand	107	1	6
α-helix	111-126	16
α-helix	139-141	3
α-helix	144-172	29
α-helix	176-192	17
α-helix	202-204	3
α-helix	205-210	6

Chain D: 6 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	53-73	21
β-strand	88	1	7
β-strand	94-95	2	7
α-helix	111-126	16
α-helix	144-172	29
α-helix	176-193	18
α-helix	202-204	3
α-helix	205-210	6

Chain E: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	54-73	20
α-helix	76-78	3
β-strand	88	1	8
β-strand	94	1	8
β-strand	95	1	9
β-strand	97	1	10
β-strand	107	1	10
α-helix	111-126	16
α-helix	139-141	3
α-helix	144-172	29
α-helix	176-192	17
α-helix	198-204	7
α-helix	205-210	6

Chain F: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	54-73	20
α-helix	76-78	3
β-strand	88	1	11
β-strand	93-94	2	11
β-strand	97	1	12
β-strand	107	1	12
α-helix	111-126	16
α-helix	139-141	3
α-helix	144-165	22
α-helix	167-172	6
α-helix	176-192	17
α-helix	198-204	7
α-helix	205-210	6

Chain G: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	379-381	3	1
α-helix	392-394	3

Chain H: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	379-381	3	3
α-helix	394-397	4

7 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 1A	A, B, C, D, E, F	protein	177	Homo sapiens	Q9H8S9 (AlphaFold model)
Serine/threonine-protein kinase 3	G, H, I, J, K, L, M, N, O	protein	31	Homo sapiens	Q13188 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>5BRM_1 MOB kinase activator 1A (chains A, B, C, D, E, F)
GLRQAVMLPEGEDLNEWIAVNTVDFFNQINMLYGTITEFCTEASCPVMSAGPRYEYHWAD
GTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVY
AHIYHQHFDSVMQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLGSKDR

Sequence of entity 2 (G, H, I, J, K, L, M, N, O), FASTA

>5BRM_2 Serine/threonine-protein kinase 3 (chains G, H, I, J, K, L, M, N, O)
DEEEEDGTMKRNATSPQVQRPSFMDYFDKQD

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	6

Primary citation

Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signaling. Ni, L., Zheng, Y., Hara, M. et al. Genes Dev (2015) 29:1416-1431. DOI 10.1101/gad.264929.115 · PubMed

Other PDB entries of the same protein (UniProt Q9H8S9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4J1V 1.95 Å, Functional and structural studies of MOBKL1B, a Salvador/Warts/Hippo tumor suppressor…
1PI1 2.0 Å, Crystal structure of a human Mob1 protein; toward understanding Mob-regulated cell cycle…
4JIZ 2.1 Å, Human Mob1-phosphopeptide complex
5XQZ 2.1 Å, Structure of the MOB1-NDR2 complex
5BRK 2.3 Å, pMob1-Lats1 complex
5TWG 2.3 Å, human MOB1A bound to human MST1 phosphorylated T353 peptide
5TWH 2.5 Å, human MOB1A bound to MST1 phosphorylated T367 peptide
6MCP 2.5 Å, L. pneumophila effector kinase LegK7 (AMP-PNP bound) in complex with human MOB1A
6MCQ 2.57 Å, L. pneumophila effector kinase LegK7 in complex with human MOB1A
5TWF 3.14 Å, Regulation of protein interactions by MOB1 phosphorylation

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