MolNFT v1 · #91419 · protein

Targeting conserved water molecules: design of 4-aryl-5- CYANOPYRROLO[2,3-D]PYRIMIDINE HSP90 inhibitors using fragment-based screening and structure-based optimization

4FCQ · Heat shock protein HSP 90-alpha: “Targeting conserved water molecules: design of 4-aryl-5- CYANOPYRROLO[2,3-D]PYRIMIDINE HSP90 inhibitors using…”. X-ray diffraction, 1 ligand (2N6), 1 pocket (best druggability 0.62). MolNFT v1…

PDB: 4FCQ
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock protein HSP 90-alpha
UniProt: P07900
Ligands: 2N6
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat shock protein HSP 90-alpha	protein	208	44% helix, 23% strand	P07900

Ligands and binding sites

2N6 · 4-(2,4-dimethylphenyl)-2-(methylsulfanyl)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	178	0.62	0.83	25	2N6

Compared structures

4FCQ · Targeting conserved water molecules: Design of 4-aryl-5-cyanopyrrolo[2,3-d]pyrimidine… · 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 P07900
Elsewhere: RCSB PDB 4FCQ · PDBe 4FCQ · UniProt P07900

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.