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Structure of human MAD1 C-terminal domain reveals its involvement in kinetochore targeting

Analyse Structure of human MAD1 C-terminal domain reveals its involvement in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4DZO
Type
protein
Length
237 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mitotic spindle assembly checkpoint protein MAD1
UniProt
Q9Y6D9
Pockets
2 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMitotic spindle assembly checkpoint protein MAD1protein11757% helix, 18% strandQ9Y6D9
BMitotic spindle assembly checkpoint protein MAD1protein12058% helix, 16% strandQ9Y6D9

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1520.280.7415empty
2570.270.7319empty

Interfaces

1 interface between chains.

  • A–B · 2218 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

  • 4DZO · Structure of Human Mad1 C-terminal Domain Reveals Its Involvement in Kinetochore Targeting · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9Y6D9 · AlphaFold monomer V2.0 prediction for mitotic spindle assembly checkpoint protein MAD1… · a predicted model of the same protein · chain A against A, TM-score 0.88

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