MolNFT v1 · #155555 · protein

Cryo-EM structure of the ATMLKL2 tetramer

6LBA · Protein kinase family protein: “Cryo-EM structure of the ATMLKL2 tetramer”. Electron microscopy, 20 pockets (best druggability 0.78). MolNFT v1 #155555 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6LBA
Type: protein
Length: 1,864 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein kinase family protein
UniProt: Q9FGG5
Pockets: 20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 55% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, B, D	Protein kinase family protein	protein	466	55% helix, 1% strand	Q9FGG5

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	629	0.78	0.83	38	empty
2	645	0.77	0.82	38	empty
3	912	0.71	0.76	91	empty
4	578	0.68	0.78	63	empty
5	552	0.68	0.78	58	empty

Interfaces

6 interfaces between chains.

C–D · 1206 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 1202 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 963 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 938 Å² buried · 10 hydrogen bonds · protein-protein
C–B · 426 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6LBA · Cryo-EM structure of the AtMLKL2 tetramer · 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 Q9FGG5
Elsewhere: RCSB PDB 6LBA · PDBe 6LBA · UniProt Q9FGG5

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