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Mm-cpn rls with ATP

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

PDB: 3IZI
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 0.82

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	738	0.82	0.85	100	empty
2	922	0.81	0.83	132	empty
3	623	0.81	0.86	82	empty
4	292	0.81	0.92	46	empty
5	281	0.80	0.92	47	empty

Interfaces

40 interfaces between chains.

L–M · 2376 Å² buried · 31 hydrogen bonds · protein-protein
G–H · 2375 Å² buried · 31 hydrogen bonds · protein-protein
C–D · 2374 Å² buried · 31 hydrogen bonds · protein-protein
I–P · 2374 Å² buried · 31 hydrogen bonds · protein-protein
D–E · 2373 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

3IZI · Mm-cpn rls with ATP · the same entry in another collection · chain D against D, 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 3IZI · PDBe 3IZI · UniProt Q877G8

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