2KYL: MAST2-PDZ

Solution structure of MAST2-PDZ complexed with the C-terminus of PTEN. Determined by solution NMR. Released 8 Jun 2011.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 845
Mol. weight: 12.01 kDa
Released: 8 Jun 2011

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

Secondary structure: helices and β-sheets

2KYL contains 4 α-helices and 9 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: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	6	1
β-strand	7-11	5	1
α-helix	12	1
β-strand	13	1	2
β-strand	16	1	2
β-strand	19-27	9	3
β-strand	34-43	10	3
α-helix	48-52	5
β-strand	59-63	5	1
β-strand	66-67	2	1
α-helix	73-82	10
β-strand	86-92	7	1

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	105-108	4	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Microtubule-associated serine/threonine-protein kinase 2	A	protein	96	Homo sapiens	Q6P0Q8 (AlphaFold model)
C-terminus of Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein…	B	protein	13		P60484 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2KYL_1 Microtubule-associated serine/threonine-protein kinase 2 (chains A)
GGSMRPPIIIHRAGKKYGFTLRAIRVYMGDSDVYTVHHMVWHVEDGGPASEAGLRQGDLI
THVNGEPVHGLVHTEVVELILKSGNKVAISTTPLEN

Sequence of entity 2 (B), FASTA

>2KYL_2 C-terminus of Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (chains B)
PFDEDQHTQITKV

Primary citation

Solution structure of MAST2-PDZ complexed with the C-terminus of PTEN. Terrien, E., Wolff, N., Cordier, F. et al. To be published.

Other PDB entries of the same protein (UniProt Q6P0Q8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2KQF Solution structure of MAST205-PDZ complexed with the C-terminus of a rabies virus G…

Browse structure collections

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