Research workbench
Solution structure of the phd domain in ring finger protein 107
Analyse Solution structure of the phd domain in ring finger protein 107 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E6S
- Type
- protein
- Length
- 77 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase UHRF2
- EC
- 6.3.2.-
- UniProt
- Q96PU4
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 0% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase UHRF2 (EC 6.3.2.-) | protein | 77 | 0% helix, 8% strand | Q96PU4 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2E6S · Solution structure of the PHD domain in RING finger protein 107 · the same entry in another collection · chain A against A, TM-score 1.00
- Q96PU4 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase UHRF2 (Q96PU4) · a predicted model of the same protein · chain A against A, TM-score 0.74
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 Q96PU4
- Elsewhere: RCSB PDB 2E6S · PDBe 2E6S · UniProt Q96PU4
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