Research workbench
Structure of UHRF1 in complex with unmodified H3 N-terminal tail
Analyse Structure of UHRF1 in complex with unmodified H3 N-terminal tail in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3T6R
- Type
- protein
- Length
- 143 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase UHRF1; Histone H3.1T N-terminal peptide
- UniProt
- Q96T88, Q16695
- Ligands
- ZN, MG
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase UHRF1 | protein | 70 | 4% helix, 10% strand | Q96T88 |
| B | E3 ubiquitin-protein ligase UHRF1 | protein | 68 | 9% helix, 9% strand | Q96T88 |
| D | Histone H3.1T N-terminal peptide | protein | 5 | 0% helix, 20% strand | Q16695 |
Ligands and binding sites
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 385 | 0.55 | 0.74 | 51 | empty |
Interfaces
3 interfaces between chains.
- B–D · 452 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 436 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 88 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3T6R · Structure of UHRF1 in complex with unmodified H3 N-terminal tail · the same entry in another collection · chain A against A, TM-score 1.00
- Q96T88 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase UHRF1 (Q96T88) · a predicted model of the same protein · chain A against A, TM-score 0.92
- Q16695 · AlphaFold monomer V2.0 prediction for histone H3.1T (Q16695) · a predicted model of the same protein · chain D against A, TM-score 0.83
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 Q96T88
- Every structure of UniProt Q16695
- Elsewhere: RCSB PDB 3T6R · PDBe 3T6R · UniProt Q96T88 · UniProt Q16695
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