MolNFT v1 · #61086 · protein
Crystal structure of the tandem tudor domains of the E3 ubiquitin- protein ligase UHRF1
3DB4 · E3 ubiquitin-protein ligase UHRF1: “Crystal structure of the tandem tudor domains of the E3 ubiquitin- protein ligase UHRF1”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #61086 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 3DB4
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase UHRF1
- EC
- 6.3.2.-
- UniProt
- Q96T88
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase UHRF1 (EC 6.3.2.-) | protein | 135 | 4% helix, 49% strand | Q96T88 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 3DB4 · Crystal structure of the tandem tudor domains of the E3 ubiquitin-protein ligase UHRF1 · 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 0.97
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
- Elsewhere: RCSB PDB 3DB4 · PDBe 3DB4 · UniProt Q96T88
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