Research workbench

Solution Structure of the oligomerization domain in Dmp53

Analyse Solution Structure of the oligomerization domain in Dmp53 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RP4
Type: protein
Length: 284 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: NOT
Source: Drosophila melanogaster
Molecule: Transcription factor p53
UniProt: Q9N6D8
Pockets: 2 · best druggability 0.50

Structure

solution nmr · resolution NOT · 1 distinct chain · 56% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Transcription factor p53	protein	71	56% helix, 15% strand	Q9N6D8

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	193	0.50	0.76	33	empty
2	79	0.34	0.75	19	empty

Interfaces

6 interfaces between chains.

C–D · 2006 Å² buried · 27 hydrogen bonds · protein-protein
A–B · 1993 Å² buried · 27 hydrogen bonds · protein-protein
B–C · 545 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 537 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 64 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2RP4 · Solution structure of the oligomerization domain in DMP53 · 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 Q9N6D8
Elsewhere: RCSB PDB 2RP4 · PDBe 2RP4 · UniProt Q9N6D8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.