Research workbench
An extended conformation of the rwd domain of human ring finger protein 25
Analyse An extended conformation of the rwd domain of human ring finger protein 25 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DMF
- Type
- protein
- Length
- 137 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ring finger protein 25
- EC
- 6.3.2.-
- UniProt
- Q96BH1
Structure
solution nmr · 1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ring finger protein 25 (EC 6.3.2.-) | protein | 137 | 34% helix, 20% strand | Q96BH1 |
Compared structures
- 2DMF · An extended conformation of the RWD domain of human Ring finger protein 25 · the same entry in another collection · chain A against A, TM-score 1.00
- Q96BH1 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF25 (Q96BH1) · a predicted model of the same protein · chain A against A, TM-score 0.82
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 Q96BH1
- Elsewhere: RCSB PDB 2DMF · PDBe 2DMF · UniProt Q96BH1
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