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Crystal structure of KEAP1 kelch domain (residues 322-609) in complex with 6K

Analyse Crystal structure of KEAP1 kelch domain (residues 322-609) in complex with 6K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7XM3
Type: protein
Length: 282 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: GED
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kelch-like ech-associated protein 1	protein	282	0% helix, 50% strand	Q14145

Ligands and binding sites

GED · N-[4-[(2-azanyl-2-oxidanylidene-ethyl)-[4-[(2-azanyl-2-oxidanylidene-ethyl)-(4-methoxyphenyl)sulfonyl-amino]naphthalen-1-yl]sulfamoyl]phenyl]-3-(4-ethylpiperazin-1-yl)propanamide · 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	708	0.74	0.80	52	GED

Compared structures

7XM3 · Crystal structure of Keap1 Kelch domain (residues 322-609) in complex with 6k · 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 7XM3 · PDBe 7XM3 · UniProt Q14145

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