MolNFT v1 · #131268 · 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-(4-bromo-6-morpholin-4-ylpyridin-2-yl)-3-[5-(2-methoxyethyl)-4- methylthiophen-2-YL]SULFONYLUREA

5Q07: “Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed…”. X-ray diffraction, 1 ligand (95Y), 20 pockets (best druggability 0.84). MolNFT v1 #131268 on GenesisL1: 3D structure…

PDB: 5Q07
Type: protein
Length: 2,540 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-1,6-bisphosphatase 1
EC: 3.1.3.11
UniProt: Q2TU34
Ligands: 95Y
Pockets: 20 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E	Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11)	protein	319	39% helix, 25% strand	Q2TU34
B, C, D, F, G, H	Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11)	protein	317	39% helix, 26% strand	Q2TU34

Ligands and binding sites

95Y · N-{[4-bromo-6-(morpholin-4-yl)pyridin-2-yl]carbamoyl}-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide · ligand · 8 copies · chains A, C, B, D, E, G, F, 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, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	927	0.84	0.85	97	empty
2	719	0.83	0.86	76	empty
3	793	0.73	0.78	88	empty
4	395	0.67	0.80	45	95Y
5	390	0.66	0.79	46	95Y

Interfaces

14 interfaces between chains.

A–B · 2421 Å² buried · 36 hydrogen bonds · protein-protein
G–H · 2386 Å² buried · 28 hydrogen bonds · protein-protein
C–D · 2366 Å² buried · 32 hydrogen bonds · protein-protein
E–F · 2344 Å² buried · 36 hydrogen bonds · protein-protein
F–H · 1332 Å² buried · 27 hydrogen bonds · protein-protein

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 Q2TU34
Elsewhere: RCSB PDB 5Q07 · PDBe 5Q07 · UniProt Q2TU34

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