Research workbench

Yeast HSP90 N-terminal domain li-IV mutant with radicicol

Analyse Yeast HSP90 N-terminal domain li-IV mutant with radicicol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WER
Type: protein
Length: 428 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent molecular chaperone HSP82
UniProt: P02829
Ligands: RDC
Pockets: 1 · best druggability 0.78

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ATP-dependent molecular chaperone HSP82	protein	214	42% helix, 22% strand	P02829

Ligands and binding sites

RDC · Radicicol · ligand · 2 copies · chains A, B

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	1126	0.78	0.79	110	RDC

Interfaces

1 interface between chains.

A–B · 586 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2WER · Yeast Hsp90 N-terminal domain LI-IV mutant with Radicicol · the same entry in another collection · chain A against A, TM-score 1.00
P02829 · AlphaFold monomer V2.0 prediction for ATP-dependent molecular chaperone HSP82 (P02829) · a predicted model of the same protein · chain A against A, TM-score 0.82

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 P02829
Elsewhere: RCSB PDB 2WER · PDBe 2WER · UniProt P02829

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