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Mm-cpn rls with ATP and alfx

Analyse Mm-cpn rls with ATP and alfx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IZJ
Type: protein
Length: 8,208 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperonin
UniProt: Q877G8
Pockets: 20 · best druggability 0.84

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, O, P	Chaperonin	protein	513	53% helix, 18% 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	560	0.84	0.90	85	empty
2	682	0.83	0.87	85	empty
3	656	0.83	0.87	88	empty
4	682	0.83	0.87	82	empty
5	553	0.82	0.88	83	empty

Interfaces

40 interfaces between chains.

I–J · 2618 Å² buried · 29 hydrogen bonds · protein-protein
A–H · 2618 Å² buried · 29 hydrogen bonds · protein-protein
C–D · 2616 Å² buried · 29 hydrogen bonds · protein-protein
N–O · 2615 Å² buried · 29 hydrogen bonds · protein-protein
F–G · 2613 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

3IZJ · Mm-cpn rls with ATP and AlFx · 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 3IZJ · PDBe 3IZJ · UniProt Q877G8

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