Research workbench

Michaelis complex of fructose-2,6-bisphosphatase

Analyse Michaelis complex of fructose-2,6-bisphosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1C81
Type: protein
Length: 191 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-2,6-bisphosphatase
EC: 3.1.3.46
UniProt: P07953
Ligands: FDQ
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-2,6-bisphosphatase (EC 3.1.3.46)	protein	191	41% helix, 16% strand	P07953

Ligands and binding sites

FDQ · 2,5-anhydro-1-deoxy-1-phosphono-6-O-phosphono-D-glucitol · ligand · 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	268	0.62	0.80	35	FDQ

Compared structures

1C81 · Michaelis complex of fructose-2,6-bisphosphatase · the same entry in another collection · chain A against A, TM-score 1.00
P07953 · AlphaFold monomer V2.0 prediction for 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase… · a predicted model of the same protein · chain A 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 P07953
Elsewhere: RCSB PDB 1C81 · PDBe 1C81 · UniProt P07953

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