Research workbench
Solution NMR structure of H2H3 domain of ovine prion protein (residues 167-234)
Analyse Solution NMR structure of H2H3 domain of ovine prion protein (residues 167-234) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KTM
- Type
- protein
- Length
- 68 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major prion protein
- UniProt
- Q072G4
Structure
solution nmr · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major prion protein | protein | 68 | 78% helix, 0% strand | Q072G4 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2KTM · Solution NMR structure of H2H3 domain of ovine prion protein (residues 167-234) · 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 Q072G4
- Elsewhere: RCSB PDB 2KTM · PDBe 2KTM · UniProt Q072G4
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