Research workbench
Solution structure of the tandem hmg box domain from human high mobility group protein B1
Analyse Solution structure of the tandem hmg box domain from human high mobility group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YRQ
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High mobility group protein B1
- UniProt
- P09429
Structure
solution nmr · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High mobility group protein B1 | protein | 173 | 63% helix, 0% strand | P09429 |
Compared structures
- 2YRQ · Solution structure of the tandem HMG box domain from Human High mobility group protein B1 · the same entry in another collection · chain A against A, TM-score 1.00
- P09429 · AlphaFold monomer V2.0 prediction for high mobility group protein B1 (P09429) · a predicted model of the same protein · chain A against A, TM-score 0.43
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 P09429
- Elsewhere: RCSB PDB 2YRQ · PDBe 2YRQ · UniProt P09429
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