Research workbench
The solution structure and dynamics of the DNA binding domain of hmg-D from drosophila melanogaster
Analyse The solution structure and dynamics of the DNA binding domain of hmg-D from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HMA
- Type
- protein
- Length
- 73 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hmg-D
- UniProt
- Q05783
Structure
solution nmr · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hmg-D | protein | 73 | 71% helix, 0% strand | Q05783 |
Compared structures
- 1HMA · The solution structure and dynamics of the DNA binding domain of hmg-D from drosophila… · the same entry in another collection · chain A against A, TM-score 1.00
- Q05783 · AlphaFold monomer V2.0 prediction for high mobility group protein D (Q05783) · a predicted model of the same protein · chain A against A, TM-score 0.64
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 Q05783
- Elsewhere: RCSB PDB 1HMA · PDBe 1HMA · UniProt Q05783
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