Research workbench

Fructose-6-phosphate aldolase

Analyse Fructose-6-phosphate aldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1L6W
Type: protein
Length: 2,200 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-6-phosphate aldolase 1
EC: 4.1.2.-
UniProt: P78055
Pockets: 20 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	Fructose-6-phosphate aldolase 1 (EC 4.1.2.-)	protein	220	53% helix, 17% strand	P78055

Ligands and binding sites

GOL · Glycerol · additive · 10 copies · chains A, B, C, D, E, F, G, H, I, J

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

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	223	0.76	0.90	39	empty
2	216	0.76	0.91	33	empty
3	199	0.75	0.90	35	empty
4	203	0.74	0.90	35	empty
5	218	0.74	0.89	34	empty

Interfaces

25 interfaces between chains.

A–E · 1617 Å² buried · 11 hydrogen bonds · protein-protein
F–J · 1561 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 1560 Å² buried · 5 hydrogen bonds · protein-protein
H–I · 1560 Å² buried · 7 hydrogen bonds · protein-protein
G–H · 1558 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 covalent (additive adduct).

Compared structures

1L6W · Fructose-6-phosphate aldolase · the same entry in another collection · chain J against J, TM-score 1.00
P78055 · AlphaFold monomer V2.0 prediction for fructose-6-phosphate aldolase 1 (P78055) · a predicted model of the same protein · chain J against A, TM-score 0.99

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 P78055
Elsewhere: RCSB PDB 1L6W · PDBe 1L6W · UniProt P78055

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