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Crystal structure of F16BP aldolase from toxoplasma gondii (TGALD1)

Analyse Crystal structure of F16BP aldolase from toxoplasma gondii (TGALD1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4D2J
Type: protein
Length: 338 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: S8GE25
Ligands: SO4
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-bisphosphate aldolase (EC 4.1.2.13)	protein	338	49% helix, 16% strand	S8GE25

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
ACT · Acetate ion · additive · 2 copies · chains A
BME · Beta-mercaptoethanol · additive · 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	263	0.58	0.79	29	SO4
2	103	0.48	0.81	26	empty

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

4D2J · Crystal structure of F16BP Aldolase from Toxoplasma gondii (TgALD1) · 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 S8GE25
Elsewhere: RCSB PDB 4D2J · PDBe 4D2J · UniProt S8GE25

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