MolNFT v1 · #71338 · protein

Crystal structure of fructose bisphosphate aldolase from encephalitozoon cuniculi, bound to phosphate

3MBD · Fructose-bisphosphate aldolase: “Crystal structure of fructose bisphosphate aldolase from encephalitozoon cuniculi, bound to phosphate”. X-ray diffraction, 2 ligands (PO4, CL), 1 pocket (best druggability 0.62). MolNFT v1 #71338 on…

PDB: 3MBD
Type: protein
Length: 336 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: Q8SSM8
Ligands: PO4, CL
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-bisphosphate aldolase (EC 4.1.2.13)	protein	336	51% helix, 17% strand	Q8SSM8

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
CL · Chloride ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	232	0.62	0.82	31	PO4, CL

Compared structures

3MBD · Crystal structure of fructose bisphosphate aldolase from Encephalitozoon cuniculi, bound… · the same entry in another collection · chain A against A, TM-score 1.00
Q8SSM8 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase (Q8SSM8) · a predicted model of the same protein · 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 Q8SSM8
Elsewhere: RCSB PDB 3MBD · PDBe 3MBD · UniProt Q8SSM8

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