4GEH: MST4 dimerization domain complex with PDCD10

Crystal structure of MST4 dimerization domain complex with PDCD10. Determined by X-ray diffraction at 1.95 Å resolution. Released 17 Apr 2013.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,399
Mol. weight: 67.93 kDa
Released: 17 Apr 2013

Explore 4GEH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GEH contains 38 α-helices and 0 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: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	17-19	3
α-helix	20-21	2
α-helix	22-26	5
α-helix	27-34	8
α-helix	38-54	17
α-helix	58-69	12
α-helix	76-82	7
α-helix	88-91	4
α-helix	98-115	18
α-helix	117-120	4
α-helix	124-151	28
α-helix	157-184	28
α-helix	187-208	22

Chain B: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	352	1
α-helix	353-357	5
α-helix	358-366	9
α-helix	372-391	20
α-helix	395-409	15

Chain C: 14 helices, 0 β-strands

Element	Residues	Length
α-helix	17-19	3
α-helix	20-21	2
α-helix	22-26	5
α-helix	27-33	7
α-helix	38-54	17
α-helix	58-69	12
α-helix	76-82	7
α-helix	83-85	3
α-helix	88-91	4
α-helix	98-115	18
α-helix	117-120	4
α-helix	124-151	28
α-helix	157-184	28
α-helix	187-208	22

Chain D: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	345-350	6
α-helix	352	1
α-helix	353-357	5
α-helix	358-366	9
α-helix	372-391	20
α-helix	395-408	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Programmed cell death protein 10	A, C	protein	207	Homo sapiens	Q9BUL8 (AlphaFold model)
Serine/threonine-protein kinase MST4	B, D	protein	91	Homo sapiens	Q9P289 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4GEH_1 Programmed cell death protein 10 (chains A, C)
GMAKNEAETTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGLTQDIIMK
ILEKKSVEVNFTESLLRMAADDVEEYMIERPEPEFQDLNEKARALKQILSKIPDEINDRV
RFLQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTLKTYFKDG
KAINVFVSANRLIHQTNLILQTFKTVA

Sequence of entity 2 (B, D), FASTA

>4GEH_2 Serine/threonine-protein kinase MST4 (chains B, D)
MGSFTTVRKKPDPKKVQNGAEQDLVQTLSCLSMIITPAFAELKQQDENNASRNQAIEELE
KSIAVAEAACPGITDKMVKKLIEKFQKCSAD

Primary citation

Structural mechanism of CCM3 heterodimerization with GCKIII kinases. Zhang, M., Dong, L., Shi, Z. et al. Structure (2013) 21:680-688. DOI 10.1016/j.str.2013.02.015 · PubMed

Other PDB entries of the same protein (UniProt Q9BUL8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3AJM 2.3 Å, Crystal structure of programmed cell death 10 in complex with inositol…
3W8I 2.4 Å, Crystal structure of CCM3 in complex with the C-terminal regulatory domain of MST4
3W8H 2.43 Å, Crystal structure of CCM3 in complex with the C-terminal regulatory domain of STK25
3L8I 2.5 Å, Crystal structure of CCM3, a cerebral cavernous malformation protein critical for…
3RQG 2.5 Å, Cerebral cavernous malformation 3 (CCM3) in complex with paxillin LD4
3RQF 2.7 Å, Cerebral cavernous malformation 3 (CCM3) in complex with paxillin LD2
3RQE 2.8 Å, Cerebral cavernous malformation 3 (CCM3) in complex with paxillin LD1
4TVQ 2.8 Å, CCM3 in complex with CCM2 LD-like motif
3L8J 3.05 Å, Crystal structure of CCM3, a cerebral cavernous malformation protein critical for…

Browse structure collections

About this viewer

MolViewer shows 4GEH 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.