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A novel structure-based mechanism for DNA-binding of SATB1
Analyse A novel structure-based mechanism for DNA-binding of SATB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Q2J
- Type
- protein
- Length
- 524 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding protein SATB1
- UniProt
- Q60611
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-binding protein SATB1 | protein | 169 | 40% helix, 20% strand | Q60611 |
| B | DNA-binding protein SATB1 | protein | 94 | 32% helix, 37% strand | Q60611 |
| C | DNA-binding protein SATB1 | protein | 92 | 16% helix, 38% strand | Q60611 |
| D | DNA-binding protein SATB1 | protein | 169 | 40% helix, 21% strand | Q60611 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1063 | 0.75 | 0.78 | 90 | empty |
| 2 | 55 | 0.32 | 0.77 | 18 | empty |
| 3 | 51 | 0.30 | 0.76 | 18 | empty |
| 4 | 56 | 0.27 | 0.74 | 15 | empty |
Interfaces
4 interfaces between chains.
- A–B · 795 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 652 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 549 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 496 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 Q60611
- Elsewhere: RCSB PDB 4Q2J · PDBe 4Q2J · UniProt Q60611
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