MolNFT v1 · #179326 · protein

Kelch domain of human KEAP1 bound to NRF2 peptide, adeetgefl

7K28 · Kelch-like ech-associated protein 1: “Kelch domain of human KEAP1 bound to NRF2 peptide, adeetgefl”. X-ray diffraction, 6 pockets (best druggability 0.73). MolNFT v1 #179326 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 7K28
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 PEPTIDE,ADEETGEFL
UniProt: Q14145
Pockets: 6 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Kelch-like ech-associated protein 1	protein	284	0% helix, 52% strand	Q14145
P	NRF2 PEPTIDE,ADEETGEFL	protein	9	0% helix, 0% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	558	0.73	0.81	54	empty
2	567	0.73	0.81	57	empty
3	93	0.46	0.80	26	empty
4	91	0.43	0.79	20	empty
5	87	0.38	0.76	23	empty

Interfaces

2 interfaces between chains.

A–B · 591 Å² buried · 7 hydrogen bonds · protein-protein
B–P · 518 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

7K28 · Kelch domain of human KEAP1 bound to Nrf2 peptide, ADEETGEFL · 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 7K28 · PDBe 7K28 · UniProt Q14145

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