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Structural basis for the defects of human lung cancer somatic mutations in the repression activity of KEAP1 on NRF2

Analyse Structural basis for the defects of human lung cancer somatic mutations in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1X2J
Type: protein
Length: 290 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kelch-like ech-associated protein 1
UniProt: Q9Z2X8
Ligands: SO4
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 1% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kelch-like ech-associated protein 1	protein	290	1% helix, 49% strand	Q9Z2X8

Ligands and binding sites

SO4 · Sulfate ion · ion · 8 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	594	0.73	0.81	50	SO4

Compared structures

1X2J · Structural basis for the defects of human lung cancer somatic mutations in the repression… · the same entry in another collection · chain A against A, TM-score 1.00
Q9Z2X8 · AlphaFold monomer V2.0 prediction for kelch-like ech-associated protein 1 (Q9Z2X8) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9Z2X8
Elsewhere: RCSB PDB 1X2J · PDBe 1X2J · UniProt Q9Z2X8

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