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Truncated tetramerization domain of zebrafish P53 (crystal form I)

Analyse Truncated tetramerization domain of zebrafish P53 (crystal form I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CZ5
Type
protein
Length
118 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cellular tumor antigen P53
UniProt
G1K2L5
Pockets
1 · best druggability 0.27

Structure

x-ray diffraction · 3 distinct chains · 56% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DCellular tumor antigen P53protein2955% helix, 24% strandG1K2L5
BCellular tumor antigen P53protein2861% helix, 25% strandG1K2L5
CCellular tumor antigen P53protein3253% helix, 22% strandG1K2L5

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.270.7413empty

Interfaces

6 interfaces between chains.

  • C–D · 1375 Ų buried · 22 hydrogen bonds · protein-protein
  • A–B · 1166 Ų buried · 19 hydrogen bonds · protein-protein
  • A–D · 329 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 313 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 183 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4CZ5 · Truncated tetramerization domain of zebrafish p53 (crystal form I) · the same entry in another collection · chain A against A, TM-score 1.00

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