MolNFT v1 · #58080 · protein
Structure of UHRF1 in complex with histone tail
3ASK · E3 ubiquitin-protein ligase UHRF1: “Structure of UHRF1 in complex with histone tail”. X-ray diffraction, 2 ligands (M3L, ZN), 7 pockets (best druggability 0.74). MolNFT v1 #58080 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 3ASK
- Type
- protein
- Length
- 749 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase UHRF1; Histone H3.3
- EC
- 6.3.2.-
- UniProt
- Q96T88, P84243
- Ligands
- M3L, ZN
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · 6 distinct chains · 6% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase UHRF1 (EC 6.3.2.-) | protein | 213 | 6% helix, 33% strand | Q96T88 |
| B | E3 ubiquitin-protein ligase UHRF1 (EC 6.3.2.-) | protein | 211 | 6% helix, 35% strand | Q96T88 |
| C | E3 ubiquitin-protein ligase UHRF1 (EC 6.3.2.-) | protein | 154 | 6% helix, 43% strand | Q96T88 |
| D | E3 ubiquitin-protein ligase UHRF1 (EC 6.3.2.-) | protein | 152 | 6% helix, 42% strand | Q96T88 |
| P | Histone H3.3 | protein | 10 | 0% helix, 10% strand | P84243 |
| Q | Histone H3.3 | protein | 9 | 44% helix, 11% strand | P84243 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 815 | 0.74 | 0.78 | 73 | empty |
| 2 | 1150 | 0.71 | 0.75 | 92 | empty |
| 3 | 208 | 0.67 | 0.86 | 30 | empty |
| 4 | 247 | 0.66 | 0.83 | 35 | empty |
| 5 | 461 | 0.60 | 0.75 | 51 | empty |
Interfaces
6 interfaces between chains.
- A–P · 824 Ų buried · 10 hydrogen bonds · protein-protein
- B–Q · 763 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 669 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 650 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 479 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (methylation).
Compared structures
- 3ASK · Structure of UHRF1 in complex with histone tail · the same entry in another collection · chain Q against Q, 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 D against A, TM-score 0.98
- P84243 · AlphaFold monomer V2.0 prediction for histone H3.3 (P84243) · a predicted model of the same protein · chain Q against A, TM-score 0.58
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 P84243
- Elsewhere: RCSB PDB 3ASK · PDBe 3ASK · UniProt Q96T88 · UniProt P84243
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