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Structure of the open conformation of CTTEL1

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

PDB: 6SL1
Type: protein
Length: 2,652 residues
Chains: 1
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 · 60% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase TEL1 (EC 2.7.11.1)	protein	2652	60% helix, 2% strand	G0S4S9

Ligands and binding sites

AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	825	0.82	0.84	87	empty
2	913	0.78	0.81	101	empty
3	1044	0.77	0.79	95	empty
4	596	0.74	0.81	58	empty
5	237	0.72	0.87	30	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6SL1 · Structure of the open conformation 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 6SL1 · PDBe 6SL1 · UniProt G0S4S9

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