Research workbench
Structure of the C-terminal domain of human RNF2/RING1B;
Analyse Structure of the C-terminal domain of human RNF2/RING1B; in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H8H
- Type
- protein
- Length
- 92 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase RING2
- EC
- 6.3.2.-
- UniProt
- Q99496
- Ligands
- SO4, CL
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RING2 (EC 6.3.2.-) | protein | 92 | 28% helix, 30% strand | Q99496 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
- CL · Chloride ion · ion · chains A
- 2PE · Nonaethylene glycol · additive · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3H8H · Structure of the C-terminal domain of human RNF2/RING1B; · the same entry in another collection · chain A against A, TM-score 1.00
- Q99496 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RING2 (Q99496) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q99496
- Elsewhere: RCSB PDB 3H8H · PDBe 3H8H · UniProt Q99496
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