Research workbench
Truncated tetramerization domain of zebrafish P53 (crystal form III)
Analyse Truncated tetramerization domain of zebrafish P53 (crystal form III) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CZ7
- Type
- protein
- Length
- 185 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular tumor antigen P53
- UniProt
- G1K2L5
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 4 distinct chains · 52% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellular tumor antigen P53 | protein | 30 | 57% helix, 23% strand | G1K2L5 |
| B | Cellular tumor antigen P53 | protein | 32 | 53% helix, 22% strand | G1K2L5 |
| C, D, F | Cellular tumor antigen P53 | protein | 31 | 52% helix, 23% strand | G1K2L5 |
| E | Cellular tumor antigen P53 | protein | 30 | 47% helix, 23% strand | G1K2L5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.45 | 0.79 | 18 | PO4 |
Interfaces
12 interfaces between chains.
- A–B · 1407 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 1340 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 1300 Ų buried · 19 hydrogen bonds · protein-protein
- D–E · 381 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 368 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4CZ7 · Truncated tetramerization domain of zebrafish p53 (crystal form III) · 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 G1K2L5
- Elsewhere: RCSB PDB 4CZ7 · PDBe 4CZ7 · UniProt G1K2L5
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