Research workbench
NMR based structure of the closed conformation of LYS48-linked di- ubiquitin using experimental global rotational diffusion tensor from NMR relaxation measurements
Analyse NMR based structure of the closed conformation of LYS48-linked di- ubiquitin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PEA
- Type
- protein
- Length
- 144 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin
- UniProt
- P62988
Structure
solution nmr · 1 distinct chain · 25% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ubiquitin | protein | 72 | 25% helix, 35% strand | P62988 |
Interfaces
1 interface between chains.
- A–B · 507 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2PEA · NMR Based Structure of the Closed Conformation of LYS48-Linked Di-Ubiquitin Using… · 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 P62988
- Elsewhere: RCSB PDB 2PEA · PDBe 2PEA · UniProt P62988
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