Research workbench
Crystal structure of the human RRP6 catalytic domain with D313N mutation in the active site
Analyse Crystal structure of the human RRP6 catalytic domain with D313N mutation in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SAG
- Type
- protein
- Length
- 761 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q01780
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 381 | — | Q01780 |
| B | — | protein | 380 | — | Q01780 |
Compared structures
- 3SAG · Crystal structure of the human RRP6 catalytic domain with D313N mutation in the active… · the same entry in another collection · chain A against A, TM-score 1.00
- Q01780 · AlphaFold monomer V2.0 prediction for exosome component 10 (Q01780) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q01780
- Elsewhere: RCSB PDB 3SAG · PDBe 3SAG · UniProt Q01780
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.