MolNFT v1 · #19408 · protein

Protein aggregation and ALZHEIMER'S disease: crystallographic analysis of the phenomenon. engineered version of the ribosomal protein S6 used as a stable scaffold to study oligomerization.

1QJH · 30S ribosomal protein S6: “Protein aggregation and ALZHEIMER'S disease: crystallographic analysis of the phenomenon. engineered version…”. X-ray diffraction, 1 ligand (MG), 1 pocket (best druggability 0.34). MolNFT v1 #19408 on…

PDB: 1QJH
Type: protein
Length: 93 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 30S ribosomal protein S6
UniProt: P23370
Ligands: MG
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	30S ribosomal protein S6	protein	93	31% helix, 43% strand	P23370

Ligands and binding sites

MG · Magnesium ion · metal

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.34	0.77	18	empty

Compared structures

1QJH · Protein Aggregation and Alzheimer's Disease: Crystallographic Analysis of the Phenomenon.… · the same entry in another collection · chain A against A, TM-score 1.00
P23370 · AlphaFold monomer V2.0 prediction for 30S ribosomal protein S6 (P23370) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 P23370
Elsewhere: RCSB PDB 1QJH · PDBe 1QJH · UniProt P23370

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