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Groel (HSP60 class) fragment comprising residues 191-345

Analyse Groel (HSP60 class) fragment comprising residues 191-345 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JON
Type: protein
Length: 141 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Groel, HSP60 class
UniProt: P0A6F5
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Groel, HSP60 class	protein	141	36% helix, 33% strand	P0A6F5

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.32	0.76	16	empty

Compared structures

1JON · Groel (HSP60 class) fragment comprising residues 191-345 · the same entry in another collection · chain A against A, TM-score 1.00
P0A6F5 · AlphaFold monomer V2.0 prediction for 60 kda chaperonin (P0A6F5) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P0A6F5
Elsewhere: RCSB PDB 1JON · PDBe 1JON · UniProt P0A6F5

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