MolNFT v1 · #17191 · protein

High-resolution solution structure of the oligomerization domain of P53 by multi-dimensional NMR

1OLH · Tumor suppressor P53 (oligomerization domain): “High-resolution solution structure of the oligomerization domain of P53 by multi-dimensional NMR”. Solution nmr, 3 pockets (best druggability 0.43). MolNFT v1 #17191 on GenesisL1: 3D…

PDB: 1OLH
Type: protein
Length: 168 residues
Chains: 4
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor suppressor P53 (oligomerization domain)
UniProt: P04637
Pockets: 3 · best druggability 0.43

Structure

solution nmr · 1 distinct chain · 48% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Tumor suppressor P53 (oligomerization domain)	protein	42	48% helix, 12% 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	93	0.43	0.79	16	empty
2	79	0.40	0.78	15	empty
3	84	0.36	0.76	18	empty

Interfaces

6 interfaces between chains.

A–C · 1269 Å² buried · 24 hydrogen bonds · protein-protein
B–D · 1227 Å² buried · 24 hydrogen bonds · protein-protein
C–D · 368 Å² buried · 1 hydrogen bond · protein-protein
A–B · 311 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 99 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1OLH · High-resolution solution structure of the oligomerization domain of P53 by… · 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 1OLH · PDBe 1OLH · UniProt P04637

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