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HSP90 DELTA24-N210 mutant

Analyse HSP90 DELTA24-N210 mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AKP
Type: protein
Length: 365 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent molecular chaperone HSP82
UniProt: P02829
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP-dependent molecular chaperone HSP82	protein	184	40% helix, 23% strand	P02829
B	ATP-dependent molecular chaperone HSP82	protein	181	41% helix, 23% strand	P02829

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	270	0.63	0.81	25	empty
2	237	0.63	0.81	22	empty

Compared structures

2AKP · Hsp90 Delta24-N210 mutant · 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 B against A, TM-score 0.80

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 2AKP · PDBe 2AKP · UniProt P02829

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