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Crystal structure of the P14/MP1 complex at 2.15 a resolution

Analyse Crystal structure of the P14/MP1 complex at 2.15 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VEU
Type
protein
Length
242 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mitogen-activated protein kinase kinase 1 interacting protein 1; Late ENDOSOMAL/LYSOSOMAL…
UniProt
O88653, Q9JHS3

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMitogen-activated protein kinase kinase 1 interacting protein 1protein11839% helix, 31% strandO88653
BLate ENDOSOMAL/LYSOSOMAL MP1 interacting proteinprotein12440% helix, 27% strandQ9JHS3

Interfaces

1 interface between chains.

  • A–B · 1405 Ų buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

  • 1VEU · Crystal structure of the p14/MP1 complex at 2.15 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
  • O88653 · AlphaFold monomer V2.0 prediction for ragulator complex protein LAMTOR3 (O88653) · a predicted model of the same protein · chain A against A, TM-score 0.98
  • Q9JHS3 · AlphaFold monomer V2.0 prediction for ragulator complex protein LAMTOR2 (Q9JHS3) · a predicted model of the same protein · chain B against A, TM-score 0.88

Analyse

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