MolNFT v1 · #67937 · protein

Mm-cpn rls deltalid with ATP

3IZK · Chaperonin: “Mm-cpn rls deltalid with ATP”. Electron microscopy, 20 pockets (best druggability 0.87). MolNFT v1 #67937 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3IZK
Type: protein
Length: 7,856 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperonin
UniProt: Q877G8
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 1 distinct chain · 52% 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	491	52% 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	1186	0.87	0.88	124	empty
2	1070	0.87	0.88	98	empty
3	1100	0.87	0.87	98	empty
4	1179	0.86	0.87	115	empty
5	1185	0.86	0.87	113	empty

Interfaces

24 interfaces between chains.

L–M · 1175 Å² buried · 10 hydrogen bonds · protein-protein
G–H · 1174 Å² buried · 10 hydrogen bonds · protein-protein
B–C · 1170 Å² buried · 10 hydrogen bonds · protein-protein
O–P · 1170 Å² buried · 10 hydrogen bonds · protein-protein
J–K · 1169 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

3IZK · Mm-cpn rls deltalid 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 3IZK · PDBe 3IZK · UniProt Q877G8

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