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NMR solution structure of the tetrameric minimum transforming domain of P53

Analyse NMR solution structure of the tetrameric minimum transforming domain of P53 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PET
Type: protein
Length: 124 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor suppressor P53
UniProt: P04637
Pockets: 3 · best druggability 0.28

Structure

solution nmr · 1 distinct chain · 55% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Tumor suppressor P53	protein	31	55% helix, 19% strand	P04637

Pockets

3 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	51	0.28	0.75	13	empty
2	50	0.28	0.75	14	empty
3	52	0.26	0.74	11	empty

Interfaces

6 interfaces between chains.

C–D · 1217 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 1213 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 368 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 365 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 279 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1PET · NMR solution structure of the tetrameric minimum transforming domain of P53 · 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 1PET · PDBe 1PET · UniProt P04637

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