MolNFT v1 · #164029 · protein
Complete CTTEL1 dimer with C2 symmetry
6SL0 · SERINE/THREONINE-protein kinase TEL1: “Complete CTTEL1 dimer with C2 symmetry”. Electron microscopy, 2 ligands (AGS, MG), 20 pockets (best druggability 0.82). MolNFT v1 #164029 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6SL0
- Type
- protein
- Length
- 5,276 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, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | SERINE/THREONINE-protein kinase TEL1 (EC 2.7.11.1) | protein | 2638 | 64% helix, 2% 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1053 | 0.82 | 0.83 | 90 | empty |
| 2 | 1148 | 0.81 | 0.82 | 107 | empty |
| 3 | 808 | 0.80 | 0.83 | 84 | empty |
| 4 | 851 | 0.80 | 0.83 | 82 | empty |
| 5 | 548 | 0.80 | 0.86 | 78 | empty |
Interfaces
1 interface between chains.
- A–B · 3710 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6SL0 · Complete CtTel1 dimer with C2 symmetry · 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 6SL0 · PDBe 6SL0 · UniProt G0S4S9
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