Research workbench

Mitoneet bound to furosemide

Analyse Mitoneet bound to furosemide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DE9
Type: protein
Length: 75 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cdgsh iron-sulfur domain-containing protein 1
UniProt: Q9NZ45
Ligands: FES, FUN
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cdgsh iron-sulfur domain-containing protein 1	protein	75	16% helix, 12% strand	Q9NZ45

Ligands and binding sites

FES · Fe2/s2 (inorganic) cluster · ligand · chains A
FUN · 5-(aminosulfonyl)-4-chloro-2-[(2-furylmethyl) amino]benzoic acid · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.28	0.74	14	empty

Compared structures

6DE9 · mitoNEET bound to furosemide · the same entry in another collection · chain A against A, TM-score 1.00
Q9NZ45 · AlphaFold monomer V2.0 prediction for cdgsh iron-sulfur domain- containing protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.88

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 Q9NZ45
Elsewhere: RCSB PDB 6DE9 · PDBe 6DE9 · UniProt Q9NZ45

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