Research workbench
Crystal structure of P73 DNA-binding domain tetramer bound to a full response-element
Analyse Crystal structure of P73 DNA-binding domain tetramer bound to a full… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G83
- Type
- protein + DNA
- Length
- 416 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA; Tumor protein P73
- UniProt
- O15350
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, F | DNA | dna | 10 | — | — |
| A, B | Tumor protein P73 | protein | 198 | 10% helix, 33% strand | O15350 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 765 | 0.74 | 0.79 | 73 | empty |
| 2 | 127 | 0.42 | 0.76 | 17 | empty |
| 3 | 127 | 0.39 | 0.74 | 20 | empty |
| 4 | 52 | 0.35 | 0.79 | 17 | empty |
| 5 | 85 | 0.34 | 0.75 | 16 | empty |
Interfaces
6 interfaces between chains.
- E–F · 443 Ų buried · 34 hydrogen bonds · nucleic-nucleic
- F–A · 278 Ų buried · 7 hydrogen bonds · protein-nucleic
- E–B · 276 Ų buried · 8 hydrogen bonds · protein-nucleic
- A–B · 236 Ų buried · 6 hydrogen bonds · protein-protein
- F–B · 185 Ų buried · 2 hydrogen bonds · protein-nucleic
Compared structures
- 4G83 · Crystal Structure of p73 DNA-Binding Domain Tetramer bound to a Full Response-Element · the same entry in another collection · chain E against E, 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 4G83 · PDBe 4G83 · UniProt O15350
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