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Human MHF1-MHF2 complex

Analyse Human MHF1-MHF2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NE5
Type
protein
Length
668 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Centromere protein S; Centromere protein X
UniProt
Q8N2Z9, A8MT69
Pockets
7 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GCentromere protein Sprotein9381% helix, 4% strandQ8N2Z9
B, D, F, HCentromere protein Xprotein7469% helix, 5% strandA8MT69

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19880.750.7876empty
21850.540.7920empty
31700.530.7920empty
41390.490.7919empty
51410.430.7521empty

Interfaces

18 interfaces between chains.

  • G–H · 2408 Ų buried · 17 hydrogen bonds · protein-protein
  • C–D · 2400 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 2396 Ų buried · 17 hydrogen bonds · protein-protein
  • E–F · 2394 Ų buried · 16 hydrogen bonds · protein-protein
  • C–G · 549 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 4NE5 · Human MHF1-MHF2 complex · the same entry in another collection · chain H against H, TM-score 1.00
  • A8MT69 · AlphaFold monomer V2.0 prediction for centromere protein X (A8MT69) · a predicted model of the same protein · chain D against A, TM-score 0.99

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