Research workbench
Crystal structure of p63 SAM in complex with darpin A5
Analyse Crystal structure of p63 SAM in complex with darpin A5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Z72
- Type
- protein
- Length
- 222 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Homo sapiens; synthetic construct
- Molecule
- Isoform 9 of Tumor protein 63; Darpin A5
- UniProt
- Q9H3D4
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · resolution 1.8 · 2 distinct chains · 58% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 9 of Tumor protein 63 | protein | 65 | 66% helix, 3% strand | Q9H3D4 |
| B | Darpin A5 | protein | 157 | 55% helix, 0% strand | — |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.40 | 0.75 | 17 | empty |
| 2 | 86 | 0.31 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 908 Ų buried · 13 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 Q9H3D4
- Elsewhere: RCSB PDB 7Z72 · PDBe 7Z72 · UniProt Q9H3D4
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