Research workbench
P73 homo-tetramerization domain mutant I
Analyse P73 homo-tetramerization domain mutant I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HOB
- Type
- protein
- Length
- 363 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumor protein P73
- UniProt
- O15350
- Ligands
- MG
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 8 distinct chains · 66% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tumor protein P73 | protein | 45 | 69% helix, 16% strand | O15350 |
| B | Tumor protein P73 | protein | 45 | 62% helix, 16% strand | O15350 |
| C | Tumor protein P73 | protein | 46 | 61% helix, 15% strand | O15350 |
| D | Tumor protein P73 | protein | 43 | 72% helix, 16% strand | O15350 |
| E | Tumor protein P73 | protein | 48 | 65% helix, 15% strand | O15350 |
| F | Tumor protein P73 | protein | 44 | 68% helix, 16% strand | O15350 |
| G | Tumor protein P73 | protein | 47 | 64% helix, 15% strand | O15350 |
| H | Tumor protein P73 | protein | 45 | 67% helix, 16% strand | O15350 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains E, F
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 | 172 | 0.52 | 0.79 | 29 | empty |
| 2 | 98 | 0.43 | 0.78 | 25 | empty |
| 3 | 58 | 0.30 | 0.75 | 13 | empty |
Interfaces
17 interfaces between chains.
- G–H · 1235 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1180 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1153 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 1141 Ų buried · 20 hydrogen bonds · protein-protein
- E–G · 892 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5HOB · p73 homo-tetramerization domain mutant I · the same entry in another collection · chain A against A, TM-score 1.00
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 O15350
- Elsewhere: RCSB PDB 5HOB · PDBe 5HOB · UniProt O15350
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