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Crystal structure of KEAP1 soaked with synthetic small molecular

Analyse Crystal structure of KEAP1 soaked with synthetic small molecular in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VNH
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kelch-like ech-associated protein 1
UniProt: Q14145
Ligands: FUU
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kelch-like ech-associated protein 1	protein	288	0% helix, 53% strand	Q14145

Ligands and binding sites

FUU · 2-(3-((3-(5-(furan-2-yl)-1,3,4-oxadiazol-2-yl)ureido)methyl)phenoxy)acetic acid · ligand · 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	581	0.74	0.81	56	FUU

Compared structures

3VNH · Crystal Structure of Keap1 Soaked with Synthetic Small Molecular · 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 Q14145
Elsewhere: RCSB PDB 3VNH · PDBe 3VNH · UniProt Q14145

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