Research workbench
Crystal structure of human hmg box-containing protein 1, HBP1
Analyse Crystal structure of human hmg box-containing protein 1, HBP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QVE
- Type
- protein
- Length
- 389 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hmg box-containing protein 1
- UniProt
- O60381
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hmg box-containing protein 1 | protein | 130 | 14% helix, 35% strand | O60381 |
| C | Hmg box-containing protein 1 | protein | 129 | 12% helix, 36% strand | O60381 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
- EDO · 1,2-ethanediol · additive · 35 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 333 | 0.64 | 0.79 | 43 | empty |
Interfaces
2 interfaces between chains.
- A–C · 733 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 291 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3QVE · Crystal structure of human HMG box-containing protein 1, HBP1 · the same entry in another collection · chain A against A, TM-score 1.00
- O60381 · AlphaFold monomer V2.0 prediction for hmg box-containing protein 1 (O60381) · a predicted model of the same protein · chain C against A, TM-score 0.98
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 O60381
- Elsewhere: RCSB PDB 3QVE · PDBe 3QVE · UniProt O60381
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