Research workbench
Crystal structure of the C-terminal domain of mouse NRDP1
Analyse Crystal structure of the C-terminal domain of mouse NRDP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OGB
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ring finger protein 41
- EC
- 6.3.2.19
- UniProt
- Q8BH75
- Ligands
- SCN
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ring finger protein 41 (EC 6.3.2.19) | protein | 123 | 41% helix, 17% strand | Q8BH75 |
| B | Ring finger protein 41 (EC 6.3.2.19) | protein | 125 | 43% helix, 15% strand | Q8BH75 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 238 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 2OGB · Crystal structure of the C-terminal domain of mouse Nrdp1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q8BH75 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase NRDP1 (Q8BH75) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q8BH75
- Elsewhere: RCSB PDB 2OGB · PDBe 2OGB · UniProt Q8BH75
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