Research workbench

Groel using cryoem

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

PDB: 5W0S
Type: protein
Length: 7,336 residues
Chains: 14
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 60 kda chaperonin
UniProt: Q6Q099
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 53% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N	60 kda chaperonin	protein	524	53% helix, 18% strand	Q6Q099

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	1165	0.81	0.83	116	empty
2	1091	0.81	0.83	111	empty
3	1098	0.81	0.82	110	empty
4	1066	0.81	0.82	104	empty
5	1042	0.79	0.81	91	empty

Interfaces

28 interfaces between chains.

L–M · 1808 Å² buried · 22 hydrogen bonds · protein-protein
E–F · 1801 Å² buried · 22 hydrogen bonds · protein-protein
H–N · 1799 Å² buried · 22 hydrogen bonds · protein-protein
H–I · 1798 Å² buried · 22 hydrogen bonds · protein-protein
A–B · 1796 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

5W0S · GroEL using cryoEM · 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
Every structure of UniProt Q6Q099
Elsewhere: RCSB PDB 5W0S · PDBe 5W0S · UniProt Q6Q099

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