MolNFT v1 · #119161 · protein

Structure of the KEAP1 kelch domain in complex with a small molecule inhibitor.

5FNQ · Kelch-like ech-associated protein 1: “Structure of the KEAP1 kelch domain in complex with a small molecule inhibitor.”. X-ray diffraction, 1 ligand (S0W), 1 pocket (best druggability 0.74). MolNFT v1 #119161 on GenesisL1: 3D…

PDB: 5FNQ
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: S0W
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kelch-like ech-associated protein 1	protein	290	0% helix, 51% strand	Q9Z2X8

Ligands and binding sites

S0W · 3-(4-chlorophenyl)propanoic 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	653	0.74	0.80	58	S0W

Compared structures

5FNQ · Structure of the Keap1 Kelch domain in complex with a small molecule inhibitor. · 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 5FNQ · PDBe 5FNQ · UniProt Q9Z2X8

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