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Fat and kinase domain of CTTEL1

Analyse Fat and kinase domain of CTTEL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SKY
Type: protein
Length: 2,824 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase TEL1
EC: 2.7.11.1
UniProt: G0S4S9
Ligands: AGS, MG
Pockets: 20 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 64% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	SERINE/THREONINE-protein kinase TEL1 (EC 2.7.11.1)	protein	1412	64% helix, 3% strand	G0S4S9

Ligands and binding sites

AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	1007	0.82	0.83	90	empty
2	1156	0.81	0.82	134	empty
3	1001	0.81	0.82	109	empty
4	888	0.80	0.83	84	empty
5	1031	0.79	0.81	90	empty

Interfaces

1 interface between chains.

A–B · 3404 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

6SKY · FAT and kinase domain of CtTel1 · 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 G0S4S9
Elsewhere: RCSB PDB 6SKY · PDBe 6SKY · UniProt G0S4S9

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