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Crystal structure of the kelch domain of human KEAP1

Analyse Crystal structure of the kelch domain of human KEAP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ROG
Type: protein
Length: 572 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kelch-like ech-associated protein 1
UniProt: Q14145
Ligands: NA
Pockets: 2 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X, A	Kelch-like ech-associated protein 1	protein	286	0% helix, 49% strand	Q14145

Ligands and binding sites

NA · Sodium ion · metal · 4 copies · chains X, A
FMT · Formic acid · additive · 9 copies · chains X, A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1079	0.86	0.87	123	FMT, NA
2	73	0.33	0.75	20	empty

Interfaces

1 interface between chains.

X–A · 578 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6ROG · Crystal Structure of the KELCH domain of human KEAP1 · the same entry in another collection · chain X against X, 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 6ROG · PDBe 6ROG · UniProt Q14145

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