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Crystal structure of fructokinase from vibrio cholerae O395 in fructose, ADP and calcium ion bound form

Analyse Crystal structure of fructokinase from vibrio cholerae O395 in fructose, ADP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5F0Z
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructokinase
EC: 2.7.1.4
UniProt: A0A0H3AER7
Ligands: ADP, FRU, CA, NA
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructokinase (EC 2.7.1.4)	protein	308	42% helix, 23% strand	A0A0H3AER7

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
FRU · beta-D-fructofuranose · sugar · chains A
CA · Calcium ion · metal · chains A
NA · Sodium 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.70	0.97	21	FRU
2	366	0.66	0.80	41	ADP, CA
3	97	0.43	0.78	16	empty

Compared structures

5F0Z · Crystal structure of Fructokinase from Vibrio cholerae O395 in fructose, ADP and calcium… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A0H3AER7
Elsewhere: RCSB PDB 5F0Z · PDBe 5F0Z · UniProt A0A0H3AER7

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