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Hexokinase from schistosoma mansoni complexed with glucose

Analyse Hexokinase from schistosoma mansoni complexed with glucose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BDG
Type: protein
Length: 444 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hexokinase
EC: 2.7.1.1
UniProt: Q26609
Ligands: GLC, SO4
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hexokinase (EC 2.7.1.1)	protein	444	43% helix, 19% strand	Q26609

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · chains A
SO4 · Sulfate ion · ion · 3 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	160	0.59	0.83	25	SO4
2	206	0.49	0.75	30	empty
3	52	0.32	0.77	15	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1BDG · Hexokinase from schistosoma mansoni complexed with glucose · the same entry in another collection · chain A against A, TM-score 1.00
Q26609 · AlphaFold monomer V2.0 prediction for hexokinase (Q26609) · 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 Q26609
Elsewhere: RCSB PDB 1BDG · PDBe 1BDG · UniProt Q26609

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