MolNFT v1 · #67939 · protein

Mm-cpn wildtype with ATP

3IZM · Chaperonin: “Mm-cpn wildtype with ATP”. Electron microscopy, 20 pockets (best druggability 0.84). MolNFT v1 #67939 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3IZM
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	538	0.84	0.90	70	empty
2	540	0.84	0.90	68	empty
3	538	0.84	0.90	69	empty
4	585	0.84	0.89	73	empty
5	534	0.84	0.90	70	empty

Interfaces

28 interfaces between chains.

I–J · 2102 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 2102 Å² buried · 19 hydrogen bonds · protein-protein
I–P · 2101 Å² buried · 19 hydrogen bonds · protein-protein
O–P · 2101 Å² buried · 19 hydrogen bonds · protein-protein
F–G · 2100 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

3IZM · Mm-cpn wildtype with ATP · 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 3IZM · PDBe 3IZM · UniProt Q877G8

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