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Solution structure of the first HMG-box domain from high mobility group protein B3
Analyse Solution structure of the first HMG-box domain from high mobility group protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EQZ
- Type
- protein
- Length
- 86 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Source
- Homo sapiens
- Molecule
- High mobility group protein B3
- UniProt
- O15347
Structure
solution nmr · resolution NOT · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High mobility group protein B3 | protein | 86 | 63% helix, 0% strand | O15347 |
Compared structures
- 2EQZ · Solution structure of the first hmg-box domain from high mobility group protein B3 · the same entry in another collection · chain A against A, TM-score 1.00
- O15347 · AlphaFold monomer V2.0 prediction for high mobility group protein B3 (O15347) · a predicted model of the same protein · chain A against A, TM-score 0.78
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 O15347
- Elsewhere: RCSB PDB 2EQZ · PDBe 2EQZ · UniProt O15347
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