Crystal structure of human tonsl and MCM2 hbds binding to a histone H3-H4 tetramer

Structure

x-ray diffraction · 4 distinct chains · 53% helix, 3% strand (DSSP).

Ligands and binding sites

• GOL · Glycerol · additive · 2 copies · chains B, D, A
• MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Interfaces

5 interfaces between chains.

• A–B · 2225 Ų buried · 17 hydrogen bonds · protein-protein
• B–C · 1258 Ų buried · 29 hydrogen bonds · protein-protein
• B–D · 1004 Ų buried · 20 hydrogen bonds · protein-protein
• A–C · 939 Ų buried · 16 hydrogen bonds · protein-protein
• A–D · 84 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 5JA4 · Crystal structure of human TONSL and MCM2 HBDs binding to a histone H3-H4 tetramer · the same entry in another collection · chain A against A, TM-score 1.00
• P84243 · AlphaFold monomer V2.0 prediction for histone H3.3 (P84243) · a predicted model of the same protein · chain A against A, TM-score 0.95
• Q96HA7 · AlphaFold monomer V2.0 prediction for tonsoku-like protein (Q96HA7) · a predicted model of the same protein · chain D against A, TM-score 0.94
• P49736 · AlphaFold monomer V2.0 prediction for DNA replication licensing factor MCM2 (P49736) · a predicted model of the same protein · chain C against A, TM-score 0.45

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P84243
• Every structure of UniProt P62805
• Every structure of UniProt P49736
• Every structure of UniProt Q96HA7
• Elsewhere: RCSB PDB 5JA4 · PDBe 5JA4 · UniProt P84243 · UniProt P62805 · UniProt P49736 · UniProt Q96HA7