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The N-arylsulfonyl-indole-2-carboxamide-based inhibitors against fructose-1,6-bisphosphatase

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PDB: 7CVN
Type: protein
Length: 1,276 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: P09467
Ligands: GJO, FBP
Pockets: 19 · best druggability 0.85

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11)	protein	318	39% helix, 25% strand	P09467
C	Fructose-1,6-bisphosphatase 1 (EC 3.1.3.11)	protein	322	38% helix, 25% strand	P09467

Ligands and binding sites

GJO · 4-(3-acetamidophenyl)-N-(4-methoxyphenyl)sulfonyl-7-nitro-1H-indole-2-carboxamide · ligand · 4 copies · chains A, C, B, D
FBP · 1,6-di-O-phosphono-beta-D-fructofuranose · ligand · 4 copies · chains A, B, C, 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, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1142	0.85	0.86	118	empty
2	94	0.77	0.98	31	empty
3	448	0.68	0.79	48	GJO
4	419	0.66	0.79	44	GJO
5	287	0.63	0.81	65	FBP

Interfaces

6 interfaces between chains.

C–D · 2428 Å² buried · 31 hydrogen bonds · protein-protein
A–B · 2416 Å² buried · 30 hydrogen bonds · protein-protein
A–C · 1087 Å² buried · 17 hydrogen bonds · protein-protein
B–D · 1065 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 459 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7CVN · The N-arylsulfonyl-indole-2-carboxamide-based inhibitors against… · the same entry in another collection · chain D against D, TM-score 1.00
P09467 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P09467) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P09467
Elsewhere: RCSB PDB 7CVN · PDBe 7CVN · UniProt P09467

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