Research workbench
Full structure of rymv P1 protein, derived from crystallographic and NMR data.
Analyse Full structure of rymv P1 protein, derived from crystallographic and NMR data. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XV2
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P1
- UniProt
- Q709H6
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 28% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | P1 | protein | 157 | 28% helix, 38% strand | Q709H6 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XV2 · Full structure of RYMV P1 protein, derived from crystallographic and NMR data. · the same entry in another collection · chain A against A, TM-score 1.00
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 Q709H6
- Elsewhere: RCSB PDB 6XV2 · PDBe 6XV2 · UniProt Q709H6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.