Research workbench

Class II fructose-1,6-bisphosphate aldolase

Analyse Class II fructose-1,6-bisphosphate aldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZEN
Type: protein
Length: 338 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Class II fructose-1,6-bisphosphate aldolase
EC: 4.1.2.13
UniProt: P0AB71
Ligands: ZN
Pockets: 4 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Class II fructose-1,6-bisphosphate aldolase (EC 4.1.2.13)	protein	338	49% helix, 12% strand	P0AB71

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

4 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	134	0.51	0.80	23	empty
2	93	0.44	0.79	22	empty
3	78	0.37	0.77	17	empty
4	69	0.33	0.76	15	empty

Compared structures

1ZEN · Class II fructose-1,6-bisphosphate aldolase · the same entry in another collection · chain A against A, TM-score 1.00
P0AB71 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase class 2 (P0AB71) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P0AB71
Elsewhere: RCSB PDB 1ZEN · PDBe 1ZEN · UniProt P0AB71

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