Research workbench
Three-dimensional solution structure of apo-S100P protein determined by NMR spectroscopy
Analyse Three-dimensional solution structure of apo-S100P protein determined by NMR… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OZO
- Type
- protein
- Length
- 190 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-100P protein
- UniProt
- P25815
Structure
solution nmr · 1 distinct chain · 55% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | S-100P protein | protein | 95 | 55% helix, 6% strand | P25815 |
Interfaces
1 interface between chains.
- A–B · 1473 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1OZO · Three-dimensional solution structure of apo-S100P protein determined by NMR spectroscopy · the same entry in another collection · chain A against A, TM-score 1.00
- P25815 · AlphaFold monomer V2.0 prediction for protein S100-P (P25815) · a predicted model of the same protein · chain A against A, TM-score 0.73
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 P25815
- Elsewhere: RCSB PDB 1OZO · PDBe 1OZO · UniProt P25815
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.