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GROEL

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

PDB: 1SS8
Type: protein
Length: 3,668 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Groel protein
UniProt: P0A6F5
Pockets: 20 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G	Groel protein	protein	524	52% helix, 19% strand	P0A6F5

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	988	0.80	0.81	109	empty
2	1133	0.78	0.80	102	empty
3	948	0.77	0.80	95	empty
4	779	0.73	0.79	68	empty
5	536	0.73	0.82	59	empty

Interfaces

7 interfaces between chains.

B–C · 1756 Å² buried · 23 hydrogen bonds · protein-protein
A–B · 1742 Å² buried · 22 hydrogen bonds · protein-protein
E–F · 1709 Å² buried · 23 hydrogen bonds · protein-protein
D–E · 1706 Å² buried · 23 hydrogen bonds · protein-protein
F–G · 1701 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

1SS8 · GroEL · the same entry in another collection · chain G against G, TM-score 1.00
P0A6F5 · AlphaFold monomer V2.0 prediction for 60 kda chaperonin (P0A6F5) · a predicted model of the same protein · chain C against A, TM-score 0.87

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 1SS8 · PDBe 1SS8 · UniProt P0A6F5

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