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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-3-methyl-1,2-thiazol-5-yl)-3-(3-METHYLPHENYL)SULFONYLUREA

Analyse Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Q0B
Type: protein
Length: 1,278 residues
Chains: 4
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: 96J
Pockets: 20 · best druggability 0.85

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11)	protein	327	39% helix, 24% strand	Q2TU34
B, C, D	Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11)	protein	317	39% helix, 25% strand	Q2TU34

Ligands and binding sites

96J · N-[(4-bromo-3-methyl-1,2-thiazol-5-yl)carbamoyl]-3-methylbenzene-1-sulfonamide · ligand · 4 copies · chains A, C, B, D

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

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1104	0.85	0.86	122	empty
2	60	0.66	0.94	30	empty
3	298	0.61	0.79	55	empty
4	329	0.60	0.77	44	96J
5	296	0.59	0.78	42	96J

Interfaces

6 interfaces between chains.

C–D · 2377 Å² buried · 30 hydrogen bonds · protein-protein
A–B · 2366 Å² buried · 34 hydrogen bonds · protein-protein
B–D · 1266 Å² buried · 29 hydrogen bonds · protein-protein
A–C · 1251 Å² buried · 26 hydrogen bonds · protein-protein
A–D · 529 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5Q0B · Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase… · the same entry in another collection · chain A against A, TM-score 1.00

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 5Q0B · PDBe 5Q0B · UniProt Q2TU34

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