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HSP90 alpha N-terminal domain in complex with a macrocyclic inhibitor

Analyse HSP90 alpha N-terminal domain in complex with a macrocyclic inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VHA
Type: protein
Length: 215 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: VHA
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat shock protein HSP 90-alpha	protein	215	42% helix, 22% strand	P07900

Ligands and binding sites

VHA · 22-methyl-13,18-dioxa-7-thia-3,5-diazatetracyclo[17.3.1.1~2,6~.1~8,12~]pentacosa-1(23),2(25),3,5,8(24),9,11,19,21-nonaen-4-amine · ligand · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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	234	0.64	0.82	31	VHA

Compared structures

3VHA · Hsp90 alpha N-terminal domain in complex with a macrocyclic inhibitor · 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 3VHA · PDBe 3VHA · UniProt P07900

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