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Crystal structure of fbp aldolase from toxoplasma gondii, equilibrium schiff base fbp complex

Analyse Crystal structure of fbp aldolase from toxoplasma gondii, equilibrium schiff… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TKP
Type: protein
Length: 349 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-bisphosphate aldolase
EC: 4.1.2.13
UniProt: Q8I8I2
Ligands: P6F
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-bisphosphate aldolase (EC 4.1.2.13)	protein	349	47% helix, 15% strand	Q8I8I2

Ligands and binding sites

P6F · 1,6-di-O-phosphono-D-fructose · ligand · chains A

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

Pockets

2 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	186	0.63	0.84	25	P6F
2	89	0.43	0.79	17	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

5TKP · Crystal structure of FBP aldolase from Toxoplasma gondii, equilibrium Schiff base FBP… · 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 Q8I8I2
Elsewhere: RCSB PDB 5TKP · PDBe 5TKP · UniProt Q8I8I2

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