Research workbench
NMR structure of cross-reactive peptides from homo sapiens
Analyse NMR structure of cross-reactive peptides from homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1S4J
- Type
- protein
- Length
- 13 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 60S acidic ribosomal protein P2
- UniProt
- P05387
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 60S acidic ribosomal protein P2 | protein | 13 | 0% helix, 0% strand | P05387 |
Compared structures
- 1S4J · NMR structure of cross-reactive peptides from Homo sapiens · the same entry in another collection · chain A against A, TM-score 1.00
- P05387 · AlphaFold monomer V2.0 prediction for 60S acidic ribosomal protein P2 (P05387) · a predicted model of the same protein · chain A against A, TM-score 0.21
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 P05387
- Elsewhere: RCSB PDB 1S4J · PDBe 1S4J · UniProt P05387
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.