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The FMN binding protein ATHAL3

Analyse The FMN binding protein ATHAL3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1E20
Type: protein
Length: 185 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Halotolerance protein HAL3
UniProt: Q9SWE5
Ligands: FMN, NI
Pockets: 1 · best druggability 0.25

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Halotolerance protein HAL3	protein	185	44% helix, 17% strand	Q9SWE5

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A
NI · Nickel (II) ion · metal · chains A
BME · Beta-mercaptoethanol · additive · 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	54	0.25	0.72	16	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1E20 · The FMN binding protein AtHal3 · the same entry in another collection · chain A against A, TM-score 1.00
Q9SWE5 · AlphaFold monomer V2.0 prediction for phosphopantothenoylcysteine decarboxylase (Q9SWE5) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9SWE5
Elsewhere: RCSB PDB 1E20 · PDBe 1E20 · UniProt Q9SWE5

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