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E20K/I59A/E72K/I92A/D126K/A142V flavodoxin from anabaena

Analyse E20K/I59A/E72K/I92A/D126K/A142V flavodoxin from anabaena in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LJP
Type: protein
Length: 168 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flavodoxin
UniProt: P0A3E0
Ligands: FMN
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flavodoxin	protein	168	35% helix, 21% strand	P0A3E0

Ligands and binding sites

FMN · Flavin mononucleotide · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.51	0.83	22	FMN

Compared structures

5LJP · E20K/I59A/E72K/I92A/D126K/A142V flavodoxin from anabaena · the same entry in another collection · chain A against A, TM-score 1.00
P0A3E0 · AlphaFold monomer V2.0 prediction for flavodoxin (P0A3E0) · a predicted model of the same protein · 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 P0A3E0
Elsewhere: RCSB PDB 5LJP · PDBe 5LJP · UniProt P0A3E0

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