Research workbench
Open protomer of human atm (ataxia telangiectasia mutated)
Analyse Open protomer 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
- 5NP1
- Type
- protein
- Length
- 2,460 residues
- Chains
- 1
- 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 0.83
Structure
electron microscopy · 1 distinct chain · 64% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine-protein kinase atm (EC 2.7.11.1) | protein | 2460 | 64% helix, 1% strand | Q13315 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 813 | 0.83 | 0.86 | 160 | empty |
| 2 | 1017 | 0.82 | 0.84 | 143 | empty |
| 3 | 951 | 0.82 | 0.83 | 159 | empty |
| 4 | 635 | 0.79 | 0.84 | 111 | empty |
| 5 | 540 | 0.76 | 0.84 | 85 | empty |
Compared structures
- 5NP1 · Open protomer 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 5NP1 · PDBe 5NP1 · UniProt Q13315
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