Research workbench

Kelch domain of human KEAP1 bound to NRF2 cyclic peptide, C[GEPETGE]

Analyse Kelch domain of human KEAP1 bound to NRF2 cyclic peptide, C[GEPETGE] in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7K2M
Type: protein
Length: 580 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kelch-like ech-associated protein 1; NRF2 cyclic PEPTIDE,C[GEPETGE]
UniProt: Q14145
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 0% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Kelch-like ech-associated protein 1	protein	289	0% helix, 49% strand	Q14145
A	Kelch-like ech-associated protein 1	protein	284	0% helix, 49% strand	Q14145
P	NRF2 cyclic PEPTIDE,C[GEPETGE]	protein	7	0% helix, 0% strand	—

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	719	0.76	0.81	81	empty
2	552	0.72	0.81	53	empty
3	120	0.52	0.81	30	empty

Interfaces

2 interfaces between chains.

B–A · 464 Å² buried · 5 hydrogen bonds · protein-protein
A–P · 433 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7K2M · Kelch domain of human KEAP1 bound to Nrf2 cyclic peptide, c[GEPETGE] · the same entry in another collection · chain B against B, 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 7K2M · PDBe 7K2M · UniProt Q14145

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.