Research workbench

Crystal structure of flhf complexed with GTP/MG(2+)

Analyse Crystal structure of flhf complexed with GTP/MG(2+) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PX3
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar biosynthesis protein flhf
UniProt: Q01960
Ligands: GTP, MG
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flagellar biosynthesis protein flhf	protein	256	43% helix, 14% strand	Q01960

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · 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	70	0.47	0.83	15	empty
2	86	0.37	0.76	19	empty
3	61	0.33	0.76	15	empty

Compared structures

2PX3 · Crystal structure of FlhF complexed with GTP/Mg(2+) · the same entry in another collection · chain A against A, TM-score 1.00
Q01960 · AlphaFold monomer V2.0 prediction for flagellar biosynthesis protein flhf (Q01960) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q01960
Elsewhere: RCSB PDB 2PX3 · PDBe 2PX3 · UniProt Q01960

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.