MolNFT v1 · #48924 · protein
Crystal structure of the miz-1 BTB/POZ domain
2Q81 · Miz-1 protein: “Crystal structure of the miz-1 BTB/POZ domain”. X-ray diffraction, 3 pockets (best druggability 0.77). MolNFT v1 #48924 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2Q81
- Type
- protein
- Length
- 457 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Miz-1 protein
- UniProt
- Q13105
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 59% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Miz-1 protein | protein | 114 | 65% helix, 9% strand | Q13105 |
| B | Miz-1 protein | protein | 115 | 57% helix, 12% strand | Q13105 |
| D | Miz-1 protein | protein | 114 | 55% helix, 12% strand | Q13105 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.77 | 0.85 | 49 | empty |
| 2 | 75 | 0.31 | 0.74 | 18 | empty |
| 3 | 62 | 0.31 | 0.75 | 17 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1321 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 1312 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 800 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 756 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 187 Ų buried · 2 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 Q13105
- Elsewhere: RCSB PDB 2Q81 · PDBe 2Q81 · UniProt Q13105
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