MolNFT v1 · #118315 · protein

Crystal structure of fructokinase from vibrio cholerae O395 in apo form

5EY7: “Crystal structure of fructokinase from vibrio cholerae O395 in apo form”. X-ray diffraction, 1 ligand (NA), 7 pockets (best druggability 0.66). MolNFT v1 #118315 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5EY7
Type: protein
Length: 598 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructokinase
EC: 2.7.1.4
UniProt: A0A0H3AER7
Ligands: NA
Pockets: 7 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructokinase (EC 2.7.1.4)	protein	307	40% helix, 24% strand	A0A0H3AER7
B	Fructokinase (EC 2.7.1.4)	protein	291	39% helix, 24% strand	A0A0H3AER7

Ligands and binding sites

NA · Sodium ion · metal · chains A

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

Pockets

7 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	503	0.66	0.77	53	empty
2	248	0.50	0.75	37	empty
3	154	0.46	0.76	24	empty
4	70	0.44	0.81	12	empty
5	113	0.43	0.77	22	empty

Interfaces

1 interface between chains.

A–B · 975 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

5EY7 · Crystal structure of Fructokinase from Vibrio cholerae O395 in apo form · the same entry in another collection · 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 A0A0H3AER7
Elsewhere: RCSB PDB 5EY7 · PDBe 5EY7 · UniProt A0A0H3AER7

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