MolNFT v1 · #131253 · 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-(3-CHLOROPHENYL)SULFONYL-3-[6-[(3-chlorophenyl) SULFONYLCARBAMOYLAMINO]HEXYL]UREA

5PZS: “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 (93Y), 19 pockets (best druggability 0.82). MolNFT v1 #131253 on GenesisL1: 3D structure…

PDB: 5PZS
Type: protein
Length: 1,271 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: 93Y
Pockets: 19 · best druggability 0.82

Structure

x-ray diffraction · 3 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	319	39% helix, 25% strand	Q2TU34
B, D	Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11)	protein	317	39% helix, 25% strand	Q2TU34
C	Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11)	protein	318	39% helix, 24% strand	Q2TU34

Ligands and binding sites

93Y · N,N'-(hexane-1,6-diyldicarbamoyl)bis(3-chlorobenzene-1-sulfonamide) · ligand · 2 copies · chains A, C, B, D

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

Pockets

19 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	713	0.82	0.86	76	empty
2	546	0.66	0.77	52	empty
3	295	0.61	0.79	39	empty
4	315	0.60	0.78	47	93Y
5	267	0.54	0.76	39	empty

Interfaces

6 interfaces between chains.

A–B · 2380 Å² buried · 31 hydrogen bonds · protein-protein
C–D · 2370 Å² buried · 38 hydrogen bonds · protein-protein
B–D · 1269 Å² buried · 23 hydrogen bonds · protein-protein
A–C · 1253 Å² buried · 24 hydrogen bonds · protein-protein
B–C · 447 Å² buried · 3 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 5PZS · PDBe 5PZS · UniProt Q2TU34

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