1VEU: P14/MP1 complex

Crystal structure of the p14/MP1 complex at 2.15 A resolution. Determined by X-ray diffraction at 2.15 Å resolution. Released 3 Aug 2004.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Mus musculus
Chains: 2
Atoms: 1,927
Mol. weight: 27.4 kDa
Released: 3 Aug 2004

Explore 1VEU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1VEU contains 13 α-helices and 10 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: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	4-10	7
α-helix	13-15	3
β-strand	19-25	7	1
β-strand	31-36	6	1
α-helix	42-45	4
α-helix	47-50	4
α-helix	52-60	9
β-strand	68-74	7	1
β-strand	78-85	8	1
β-strand	88-95	8	1
α-helix	100-118	19

Chain B: 7 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	1-3	3
α-helix	4-6	3
α-helix	7-13	7
β-strand	19-25	7	1
β-strand	31-36	6	1
α-helix	42-59	18
α-helix	60-62	3
β-strand	71-76	6	1
β-strand	79-86	8	1
β-strand	89-95	7	1
α-helix	101-116	16
α-helix	118-120	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitogen-activated protein kinase kinase 1 interacting protein 1	A	protein	124	Mus musculus	O88653 (AlphaFold model)
Late endosomal/lysosomal Mp1 interacting protein	B	protein	126	Mus musculus	Q9JHS3 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1VEU_1 Mitogen-activated protein kinase kinase 1 interacting protein 1 (chains A)
MADDLKRFLYKKLPSVEGLHAIVVSDRDGVPVIKVANDSAPEHALRPGFLSTFALATDQG
SKLGLSKNKSIICYYNTYQVVQFNRLPLVVSFIASSSANTGLIVSLEKELAPLFEELIKV
VEVS

Sequence of entity 2 (B), FASTA

>1VEU_2 Late endosomal/lysosomal Mp1 interacting protein (chains B)
GMLRPKALTQVLSQANTGGVQSTLLLNNEGSLLAYSGYGDTDARVTAAIASNIWAAYDRN
GNQAFNEDSLKFILMDCMEGRVAITRVANLLLCMYAKETVGFGMLKAKAQALVQYLEEPL
TQVAAS

Primary citation

Crystal structure of the p14/MP1 scaffolding complex: How a twin couple attaches mitogen- activated protein kinase signaling to late endosomes. Kurzbauer, R., Teis, D., De Araujo, M.E. et al. Proc Natl Acad Sci U S A (2004) 101:10984-10989. DOI 10.1073/pnas.0403435101 · PubMed

Other PDB entries of the same protein (UniProt O88653 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1VET 1.9 Å, Crystal Structure of p14/MP1 at 1.9 A resolution

Browse structure collections

About this viewer

MolViewer shows 1VEU 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.