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Crystal structure of fbp aldolase from toxoplasma gondii, ternary complex

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

PDB: 5TKC
Type: protein
Length: 348 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: 13P, G3H
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-bisphosphate aldolase (EC 4.1.2.13)	protein	348	47% helix, 16% strand	Q8I8I2

Ligands and binding sites

13P · 1,3-dihydroxyacetonephosphate · ligand · chains A
G3H · Glyceraldehyde-3-phosphate · ligand · chains A
GOL · Glycerol · additive · 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	187	0.62	0.84	27	13P, G3H, GOL
2	104	0.48	0.80	26	empty

Modifications

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

Compared structures

5TKC · Crystal structure of FBP aldolase from Toxoplasma gondii, ternary complex · 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 5TKC · PDBe 5TKC · UniProt Q8I8I2

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