Research workbench
Closed dimer of human atm (ataxia telangiectasia mutated)
Analyse Closed dimer of human atm (ataxia telangiectasia mutated) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NP0
- Type
- protein
- Length
- 5,056 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
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 1 distinct chain · 65% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Serine-protein kinase atm (EC 2.7.11.1) | protein | 2528 | 65% helix, 1% strand | Q13315 |
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 | 1150 | 0.82 | 0.83 | 145 | empty |
| 2 | 1110 | 0.82 | 0.83 | 154 | empty |
| 3 | 1171 | 0.82 | 0.83 | 150 | empty |
| 4 | 1142 | 0.81 | 0.82 | 143 | empty |
| 5 | 725 | 0.79 | 0.83 | 94 | empty |
Interfaces
1 interface between chains.
- A–B · 547 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5NP0 · Closed dimer of human ATM (Ataxia telangiectasia mutated) · 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 5NP0 · PDBe 5NP0 · UniProt Q13315
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