MolNFT v2 · #227220 · protein

E.coli GroEL apoenzyme

9C0C · 60 kDa chaperonin: “E.coli GroEL apoenzyme”. Electron microscopy at 3.41, 20 pockets (best druggability 0.79). MolNFT v2 #227220 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 9C0C
Type: protein
Length: 7,336 residues
Chains: 14
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.41
Source: Escherichia coli
Molecule: 60 kDa chaperonin
UniProt: Q548M1
Pockets: 20 · best druggability 0.79

Structure

electron microscopy · resolution 3.41 · 1 distinct chain · 52% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, N, B, H, C, I, D, J, E, K, F, L, G, M	60 kDa chaperonin	protein	524	52% helix, 17% strand	Q548M1

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	896	0.79	0.82	105	empty
2	866	0.79	0.82	99	empty
3	793	0.78	0.82	93	empty
4	734	0.77	0.82	84	empty
5	1006	0.77	0.79	97	empty

Interfaces

28 interfaces between chains.

H–I · 1608 Å² buried · 17 hydrogen bonds · protein-protein
J–K · 1607 Å² buried · 17 hydrogen bonds · protein-protein
A–G · 1606 Å² buried · 18 hydrogen bonds · protein-protein
I–K · 1604 Å² buried · 18 hydrogen bonds · protein-protein
B–C · 1591 Å² buried · 18 hydrogen bonds · protein-protein

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 Q548M1
Elsewhere: RCSB PDB 9C0C · PDBe 9C0C · UniProt Q548M1

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