MolNFT v1 · #91418 · protein

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

4FCP · Heat shock protein HSP 90-alpha: “Targetting conserved water molecules: design of 4-aryl-5-cyanopyrrolo [2,3-D] pyrimidine HSP90 inhibitors…”. X-ray diffraction, 1 ligand (42C), 3 pockets (best druggability 0.68). MolNFT v1 #91418…

PDB: 4FCP
Type: protein
Length: 416 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock protein HSP 90-alpha
UniProt: P07900
Ligands: 42C
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Heat shock protein HSP 90-alpha	protein	208	42% helix, 23% strand	P07900

Ligands and binding sites

42C · N,N-dimethyl-7H-purin-6-amine · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	312	0.68	0.82	35	42C
2	187	0.61	0.83	26	42C
3	350	0.57	0.75	45	empty

Interfaces

1 interface between chains.

A–B · 368 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4FCP · Targetting 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 4FCP · PDBe 4FCP · UniProt P07900

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