MolNFT v1 · #43128 · protein
NMR structure of UHRF1 tandem tudor domains in a complex with histone H3 peptide
2L3R: “NMR structure of UHRF1 tandem tudor domains in a complex with histone H3 peptide”. Solution nmr. MolNFT v1 #43128 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2L3R
- Type
- protein
- Length
- 172 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96T88, Q3BDD9
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 161 | — | Q96T88 |
| B | — | protein | 11 | — | Q3BDD9 |
Compared structures
- 2L3R · NMR structure of UHRF1 Tandem Tudor Domains in a complex with Histone H3 peptide · 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 0.79
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 Q3BDD9
- Elsewhere: RCSB PDB 2L3R · PDBe 2L3R · UniProt Q96T88 · UniProt Q3BDD9
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