MolNFT v1 · #131273 · protein

Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(5-bromo-1,3-thiazol-2-yl)-3-[5-(4-METHOXYPHENYL)THIOPHEN-2- YL]SULFONYLUREA and with fructose-2,6-diphosphate

5Q0C · Fructose-1,6-bisphosphatase isozyme 2: “Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed…”. X-ray diffraction, 2 ligands (96G, FDP), 20 pockets (best druggability 0.86).…

PDB: 5Q0C
Type: protein
Length: 2,618 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-1,6-bisphosphatase isozyme 2
EC: 3.1.3.11
UniProt: O00757
Ligands: 96G, FDP
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, E, F, G, H	Fructose-1,6-bisphosphatase isozyme 2 (EC 3.1.3.11)	protein	328	38% helix, 25% strand	O00757
D	Fructose-1,6-bisphosphatase isozyme 2 (EC 3.1.3.11)	protein	322	37% helix, 25% strand	O00757

Ligands and binding sites

96G · N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-5-(4-methoxyphenyl)thiophene-2-sulfonamide · ligand · 8 copies · chains A, C, B, D, E, G, F, H
FDP · 2,6-di-O-phosphono-beta-D-fructofuranose · ligand · 8 copies · chains A, B, C, D, E, F, G, H

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

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	569	0.86	0.92	52	empty
2	1145	0.84	0.85	88	empty
3	689	0.71	0.78	65	empty
4	670	0.70	0.77	74	empty
5	499	0.68	0.79	42	empty

Interfaces

13 interfaces between chains.

C–D · 2514 Å² buried · 39 hydrogen bonds · protein-protein
E–F · 2506 Å² buried · 39 hydrogen bonds · protein-protein
A–B · 2500 Å² buried · 40 hydrogen bonds · protein-protein
G–H · 2468 Å² buried · 35 hydrogen bonds · protein-protein
F–H · 1343 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

O00757 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase isozyme 2 (O00757) · a predicted model of the same protein · chain D 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 O00757
Elsewhere: RCSB PDB 5Q0C · PDBe 5Q0C · UniProt O00757

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