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P53 tetramerization domain mutant T329F Q331K

Analyse P53 tetramerization domain mutant T329F Q331K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J10
Type: protein
Length: 124 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellular tumor antigen P53
UniProt: P04637
Pockets: 2 · best druggability 0.49

Structure

solution nmr · 1 distinct chain · 68% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Cellular tumor antigen P53	protein	31	68% helix, 16% strand	P04637

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	75	0.49	0.83	20	empty
2	100	0.39	0.76	17	empty

Interfaces

6 interfaces between chains.

C–D · 1228 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 1071 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 323 Å² buried · 1 hydrogen bond · protein-protein
A–D · 320 Å² buried · 1 hydrogen bond · protein-protein
A–C · 91 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2J10 · p53 tetramerization domain mutant T329F Q331K · 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 P04637
Elsewhere: RCSB PDB 2J10 · PDBe 2J10 · UniProt P04637

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