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Crystal structure of an FMN-binding protein

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

PDB: 1EJE
Type: protein
Length: 192 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FMN-binding protein
UniProt: O26255
Ligands: FMN, NI, SO4
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FMN-binding protein	protein	192	20% helix, 40% strand	O26255

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A
NI · Nickel (II) ion · metal · 2 copies · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	167	0.47	0.76	31	SO4, FMN
2	164	0.46	0.75	27	empty
3	55	0.27	0.73	14	empty

Compared structures

1EJE · Crystal structure of an FMN-binding protein · the same entry in another collection · chain A against A, TM-score 1.00
O26255 · AlphaFold monomer V2.0 prediction for protein MTH_152 (O26255) · 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 O26255
Elsewhere: RCSB PDB 1EJE · PDBe 1EJE · UniProt O26255

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