Research workbench
Structure of nucleotide-bound TEL1/ATM
Analyse Structure of nucleotide-bound TEL1/ATM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6S8F
- Type
- protein
- Length
- 5,142 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase TEL1,SERINE/THREONINE- protein kinase…
- EC
- 2.7.11.1
- UniProt
- P38110
- Ligands
- ANP, MG
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 1 distinct chain · 58% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, H | SERINE/THREONINE-protein kinase TEL1,SERINE/THREONINE- protein kinase TEL1,SERINE/THREONINE-protein kinase TEL1, SERINE/THREONINE-protein kinase TEL1,SERINE/THREONINE-protein kinase TEL1 (EC 2.7.11.1) | protein | 2571 | 58% helix, 1% strand | P38110 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains F, H
- MG · Magnesium ion · metal · 2 copies · chains F, H
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 | 867 | 0.81 | 0.83 | 94 | empty |
| 2 | 1132 | 0.80 | 0.81 | 105 | empty |
| 3 | 1047 | 0.80 | 0.81 | 98 | empty |
| 4 | 599 | 0.79 | 0.85 | 64 | empty |
| 5 | 628 | 0.78 | 0.84 | 65 | empty |
Interfaces
1 interface between chains.
- F–H · 3198 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6S8F · Structure of nucleotide-bound Tel1/ATM · the same entry in another collection · chain F against F, 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 P38110
- Elsewhere: RCSB PDB 6S8F · PDBe 6S8F · UniProt P38110
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