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

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

PDB: 7K2F
Type: protein
Length: 577 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[GAEETGE]
UniProt: Q14145
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X, A	Kelch-like ech-associated protein 1	protein	285	0% helix, 49% strand	Q14145
C	NRF2 cyclic PEPTIDE,C[GAEETGE]	protein	7	0% helix, 0% strand	—

Pockets

5 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	632	0.75	0.82	62	empty
2	589	0.73	0.80	54	empty
3	52	0.63	0.94	17	empty
4	98	0.47	0.81	24	empty
5	66	0.39	0.79	17	empty

Interfaces

2 interfaces between chains.

X–A · 651 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 440 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

7K2F · Kelch domain of human KEAP1 bound to Nrf2 cyclic peptide, c[GAEETGE] · 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 7K2F · PDBe 7K2F · UniProt Q14145

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