Research workbench
Structure of the tpr oligomerization domain
Analyse Structure of the tpr oligomerization domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TO5
- Type
- protein
- Length
- 281 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoprotein tpr
- UniProt
- P12270
Structure
x-ray diffraction · 2 distinct chains · 93% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoprotein tpr | protein | 141 | 92% helix, 0% strand | P12270 |
| B | Nucleoprotein tpr | protein | 140 | 94% helix, 0% strand | P12270 |
Interfaces
1 interface between chains.
- A–B · 3690 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
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 P12270
- Elsewhere: RCSB PDB 5TO5 · PDBe 5TO5 · UniProt P12270
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