MolNFT v1 · #138326 · protein

Kelch domain of human KEAP1 in open unliganded conformation

5WFL · Kelch-like ech-associated protein 1: “Kelch domain of human KEAP1 in open unliganded conformation”. X-ray diffraction, 1 ligand (SO4), 5 pockets (best druggability 0.75). MolNFT v1 #138326 on GenesisL1: 3D structure, binding sites…

PDB: 5WFL
Type: protein
Length: 573 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: SO4
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kelch-like ech-associated protein 1	protein	283	0% helix, 50% strand	Q14145
B	Kelch-like ech-associated protein 1	protein	290	0% helix, 52% strand	Q14145

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A, B

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

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	748	0.75	0.80	66	SO4
2	594	0.73	0.80	59	SO4
3	79	0.52	0.84	19	empty
4	112	0.43	0.77	21	empty
5	52	0.36	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 534 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5WFL · Kelch domain of human Keap1 in open unliganded conformation · 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 5WFL · PDBe 5WFL · UniProt Q14145

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