MolNFT v1 · #187525 · protein
Human atm dimer
7SIC · Serine-protein kinase atm: “Human atm dimer”. Electron microscopy, 2 ligands (ANP, MG), 20 pockets (best druggability 0.85). MolNFT v1 #187525 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7SIC
- Type
- protein
- Length
- 5,546 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine-protein kinase atm
- EC
- 2.7.11.1
- UniProt
- Q13315
- Ligands
- ANP, MG
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 1 distinct chain · 67% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Serine-protein kinase atm (EC 2.7.11.1) | protein | 2773 | 67% helix, 2% strand | Q13315 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic 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 | 969 | 0.85 | 0.86 | 99 | empty |
| 2 | 851 | 0.83 | 0.85 | 83 | empty |
| 3 | 966 | 0.80 | 0.81 | 130 | empty |
| 4 | 966 | 0.78 | 0.80 | 96 | empty |
| 5 | 949 | 0.78 | 0.80 | 89 | empty |
Interfaces
1 interface between chains.
- A–B · 4014 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 7SIC · Human ATM Dimer · 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 Q13315
- Elsewhere: RCSB PDB 7SIC · PDBe 7SIC · UniProt Q13315
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.