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Crystal structure of the HMHF1/HMHF2 histone-fold tetramer

Analyse Crystal structure of the HMHF1/HMHF2 histone-fold tetramer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4E44
Type
protein
Length
351 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Centromere protein S; Centromere protein X
UniProt
Q8N2Z9, A8MT69
Pockets
2 · best druggability 0.58

Structure

x-ray diffraction · 3 distinct chains · 76% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACentromere protein Sprotein10481% helix, 4% strandQ8N2Z9
CCentromere protein Sprotein9776% helix, 3% strandQ8N2Z9
B, DCentromere protein Xprotein7568% helix, 5% strandA8MT69

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11650.580.8228empty
2920.340.7418empty

Interfaces

6 interfaces between chains.

  • C–D · 2385 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 2304 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 633 Ų buried · 17 hydrogen bonds · protein-protein
  • B–D · 142 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 33 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4E44 · Crystal structure of the hMHF1/hMHF2 Histone-Fold Tetramer · the same entry in another collection · chain D against D, TM-score 1.00
  • A8MT69 · AlphaFold monomer V2.0 prediction for centromere protein X (A8MT69) · a predicted model of the same protein · chain B against A, TM-score 0.98
  • Q8N2Z9 · AlphaFold monomer V2.0 prediction for centromere protein S (Q8N2Z9) · a predicted model of the same protein · chain A against A, TM-score 0.95

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