Research workbench

Atomic model of the lidless mm-cpn in the open state

Analyse Atomic model of the lidless mm-cpn in the open state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IYF
Type: protein
Length: 7,856 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperonin
UniProt: Q877G8
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 44% helix, 11% 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	Chaperonin	protein	491	44% helix, 11% strand	Q877G8

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	588	0.82	0.87	80	empty
2	866	0.82	0.84	107	empty
3	689	0.81	0.85	89	empty
4	479	0.81	0.88	64	empty
5	759	0.81	0.84	83	empty

Interfaces

24 interfaces between chains.

G–H · 1225 Å² buried · 24 hydrogen bonds · protein-protein
L–M · 1168 Å² buried · 22 hydrogen bonds · protein-protein
O–P · 1156 Å² buried · 25 hydrogen bonds · protein-protein
D–E · 1148 Å² buried · 24 hydrogen bonds · protein-protein
M–N · 1123 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

3IYF · Atomic Model of the Lidless Mm-cpn in the Open State · 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 Q877G8
Elsewhere: RCSB PDB 3IYF · PDBe 3IYF · UniProt Q877G8

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