Research workbench
Adenine-N6-DNA-methyltransferase taqi
Analyse Adenine-N6-DNA-methyltransferase taqi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ADM
- Type
- protein
- Length
- 770 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Thermus aquaticus
- Molecule
- Adenine-N6-DNA-methyltransferase taqi
- EC
- 2.1.1.72
- UniProt
- P14385
- Ligands
- SAM
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · resolution 2.6 · 1 distinct chain · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Adenine-N6-DNA-methyltransferase taqi (EC 2.1.1.72) | protein | 385 | 29% helix, 29% strand | P14385 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 823 | 0.73 | 0.78 | 79 | empty |
| 2 | 186 | 0.50 | 0.76 | 32 | SAM |
| 3 | 85 | 0.42 | 0.78 | 20 | SAM |
| 4 | 70 | 0.29 | 0.72 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 503 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 P14385
- Elsewhere: RCSB PDB 2ADM · PDBe 2ADM · UniProt P14385
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