5XQZ: MOB1-NDR2 complex

Structure of the MOB1-NDR2 complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 29 Aug 2018.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,415
Mol. weight: 61.41 kDa
Ligands: ZN
Released: 29 Aug 2018

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

Secondary structure: helices and β-sheets

5XQZ contains 29 α-helices and 8 β-strands across 4 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: 12 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	41-44	4
α-helix	47-48	2
α-helix	53-73	21
β-strand	87-88	2	1
β-strand	94-95	2	1
β-strand	97	1	2
α-helix	104-106	3
β-strand	107	1	2
α-helix	111-126	16
α-helix	138-141	4
α-helix	144-165	22
α-helix	167-172	6
α-helix	176-192	17
α-helix	198-201	4
α-helix	202-204	3
α-helix	205-211	7

Chain B: 13 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	31-33	3
α-helix	41-44	4
α-helix	47-48	2
α-helix	53-73	21
β-strand	87-88	2	3
β-strand	94-95	2	3
β-strand	97	1	4
α-helix	106	1
β-strand	107	1	4
α-helix	111-126	16
α-helix	138-141	4
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
α-helix	211-213	3

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	22-56	35
α-helix	60-83	24

Chain D: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	21-56	36
α-helix	60-83	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MOB kinase activator 1A	A, B	protein	193	Homo sapiens	Q9H8S9 (AlphaFold model)
Serine/threonine-protein kinase 38-like	C, D	protein	68	Homo sapiens	Q9Y2H1 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5XQZ_1 MOB kinase activator 1A (chains A, B)
AAHHSSGHMEATLGSGNLRQAVMLPEGEDLNEWIAVNTVDFFNQINMLYGTITEFCTEAS
CPVMSAGPRYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKN
FMSVAKTILKRLFRVYAHIYHQHFDSVMQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAP
LQELIEKLGSKDR

Sequence of entity 2 (C, D), FASTA

>5XQZ_2 Serine/threonine-protein kinase 38-like (chains C, D)
SSGHMKLTLENFYSNLILQHEERETRQKKLEVAMEEEGLADEEKKLRRSQHARKETEFLR
LKRTRLGL

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

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

Primary citation

Stable MOB1 interaction with Hippo/MST is not essential for development and tissue growth control. Kulaberoglu, Y., Lin, K., Holder, M. et al. Nat Commun (2017) 8:695-695. DOI 10.1038/s41467-017-00795-y · 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
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
5BRM 2.65 Å, Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in…
5TWF 3.14 Å, Regulation of protein interactions by MOB1 phosphorylation

Browse structure collections

About this viewer

MolViewer shows 5XQZ 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.