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Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein HSP26

Analyse Multiple distinct assemblies reveal conformational flexibility in the small… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2H53
Type: protein
Length: 2,232 residues
Chains: 24
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Small heat shock protein HSP26
Pockets: 20 · best druggability 0.53

Structure

electron microscopy · 1 distinct chain · 6% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X	Small heat shock protein HSP26	protein	93	6% helix, 49% strand	—

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	201	0.53	0.78	30	empty
2	174	0.53	0.79	30	empty
3	189	0.53	0.78	29	empty
4	182	0.53	0.79	30	empty
5	185	0.53	0.78	29	empty

Interfaces

12 interfaces between chains.

I–J · 1560 Å² buried · 37 hydrogen bonds · protein-protein
O–P · 1560 Å² buried · 37 hydrogen bonds · protein-protein
Q–R · 1557 Å² buried · 37 hydrogen bonds · protein-protein
S–T · 1557 Å² buried · 37 hydrogen bonds · protein-protein
A–B · 1555 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

2H53 · Multiple distinct assemblies reveal conformational flexibility in the small heat shock… · 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
Elsewhere: RCSB PDB 2H53 · PDBe 2H53

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