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HSP90 N-terminal domain in complex with 4-(1,3-dihydro-2H- isoindol-2-YLCARBONYL)BENZENE-1,3-diol

Analyse HSP90 N-terminal domain in complex with 4-(1,3-dihydro-2H… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K99
Type: protein
Length: 867 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat shock protein HSP 90-alpha
UniProt: P07900
Ligands: PFT
Pockets: 8 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 40% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat shock protein HSP 90-alpha	protein	218	39% helix, 24% strand	P07900
B, C	Heat shock protein HSP 90-alpha	protein	216	41% helix, 25% strand	P07900
D	Heat shock protein HSP 90-alpha	protein	217	39% helix, 25% strand	P07900

Ligands and binding sites

PFT · 4-(1,3-dihydro-2H-isoindol-2-ylcarbonyl)benzene-1,3-diol · ligand · 4 copies · chains A, B, C, D

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

Pockets

8 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	1199	0.80	0.82	90	empty
2	904	0.76	0.79	65	empty
3	253	0.62	0.80	30	PFT
4	158	0.60	0.84	28	PFT
5	155	0.59	0.83	29	PFT

Interfaces

5 interfaces between chains.

B–D · 1114 Å² buried · 21 hydrogen bonds · protein-protein
A–C · 716 Å² buried · 18 hydrogen bonds · protein-protein
A–D · 429 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 295 Å² buried · 5 hydrogen bonds · protein-protein
C–D · 11 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3K99 · HSP90 N-terminal domain in complex with 4-(1,3-dihydro-2H-isoindol-2-ylcarbonyl)benzene-1… · 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 3K99 · PDBe 3K99 · UniProt P07900

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