Research workbench
Armadillo domain of HSF2BP in complex with BRCA2 peptide
Analyse Armadillo domain of HSF2BP in complex with BRCA2 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BDX
- Type
- protein
- Length
- 951 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock factor 2-binding protein; Breast cancer type 2 susceptibility protein
- UniProt
- O75031, P51587
- Ligands
- MG
- Pockets
- 12 · best druggability 0.84
Structure
x-ray diffraction · 5 distinct chains · 64% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Heat shock factor 2-binding protein | protein | 211 | 73% helix, 0% strand | O75031 |
| B | Heat shock factor 2-binding protein | protein | 212 | 74% helix, 0% strand | O75031 |
| C | Heat shock factor 2-binding protein | protein | 213 | 71% helix, 0% strand | O75031 |
| E | Breast cancer type 2 susceptibility protein | protein | 53 | 9% helix, 6% strand | P51587 |
| F | Breast cancer type 2 susceptibility protein | protein | 51 | 16% helix, 8% strand | P51587 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 900 | 0.84 | 0.85 | 100 | empty |
| 2 | 519 | 0.70 | 0.80 | 46 | empty |
| 3 | 70 | 0.63 | 0.91 | 21 | empty |
| 4 | 94 | 0.58 | 0.86 | 23 | empty |
| 5 | 165 | 0.53 | 0.80 | 19 | empty |
Interfaces
13 interfaces between chains.
- C–E · 1656 Ų buried · 32 hydrogen bonds · protein-protein
- D–F · 1528 Ų buried · 26 hydrogen bonds · protein-protein
- A–E · 1273 Ų buried · 23 hydrogen bonds · protein-protein
- B–F · 1231 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 986 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 modified (engineered).
Compared structures
- 7BDX · Armadillo domain of HSF2BP in complex with BRCA2 peptide · the same entry in another collection · chain F against F, TM-score 1.00
- O75031 · AlphaFold monomer V2.0 prediction for heat shock factor 2-binding protein (O75031) · 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 O75031
- Every structure of UniProt P51587
- Elsewhere: RCSB PDB 7BDX · PDBe 7BDX · UniProt O75031 · UniProt P51587
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