MolNFT v1 · #70582 · protein

Atomic model of mm-cpn in the closed state

3LOS · Chaperonin: “Atomic model of mm-cpn in the closed state”. Electron microscopy, 20 pockets (best druggability 0.89). MolNFT v1 #70582 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3LOS
Type: protein
Length: 8,512 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperonin
UniProt: Q877G8
Pockets: 20 · best druggability 0.89

Structure

electron microscopy · 1 distinct chain · 38% helix, 2% 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	532	38% helix, 2% 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	698	0.89	0.93	111	empty
2	651	0.88	0.93	120	empty
3	913	0.88	0.90	136	empty
4	903	0.88	0.90	141	empty
5	1010	0.87	0.88	138	empty

Interfaces

56 interfaces between chains.

G–H · 3013 Å² buried · 42 hydrogen bonds · protein-protein
K–L · 3012 Å² buried · 42 hydrogen bonds · protein-protein
M–N · 3012 Å² buried · 42 hydrogen bonds · protein-protein
A–B · 3011 Å² buried · 42 hydrogen bonds · protein-protein
A–H · 3007 Å² buried · 43 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 disulfide (disulfide).

Compared structures

3LOS · Atomic Model of Mm-cpn in the Closed State · the same entry in another collection · chain C against C, 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 3LOS · PDBe 3LOS · UniProt Q877G8

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