MolNFT v1 · #58390 · protein

HSP90 alpha N-terminal domain in complex with an inhibitor RO1127850

3B26 · Heat shock protein HSP 90-alpha: “HSP90 alpha N-terminal domain in complex with an inhibitor RO1127850”. X-ray diffraction, 1 ligand (B2L), 4 pockets (best druggability 0.64). MolNFT v1 #58390 on GenesisL1: 3D structure, binding…

PDB: 3B26
Type: protein
Length: 419 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: B2L
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat shock protein HSP 90-alpha	protein	209	44% helix, 22% strand	P07900
B	Heat shock protein HSP 90-alpha	protein	210	43% helix, 22% strand	P07900

Ligands and binding sites

B2L · 4-(1H,3H-benzo[de]isochromen-6-yl)-6-methylpyrimidin-2-amine · ligand · chains A

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

Pockets

4 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	263	0.64	0.82	29	B2L
2	161	0.59	0.83	26	empty
3	287	0.54	0.76	39	empty
4	68	0.30	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 391 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3B26 · Hsp90 alpha N-terminal domain in complex with an inhibitor Ro1127850 · 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 3B26 · PDBe 3B26 · UniProt P07900

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