Research workbench
Structure of adenine-N6-DNA-methyltransferase taqi
Analyse Structure of 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
- 1AQJ
- Type
- protein
- Length
- 764 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenine-N6-DNA-methyltransferase taqi
- EC
- 2.1.1.72
- UniProt
- P14385
- Ligands
- SFG
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenine-N6-DNA-methyltransferase taqi (EC 2.1.1.72) | protein | 381 | 28% helix, 28% strand | P14385 |
| B | Adenine-N6-DNA-methyltransferase taqi (EC 2.1.1.72) | protein | 383 | 28% helix, 28% strand | P14385 |
Ligands and binding sites
- SFG · Sinefungin · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1086 | 0.71 | 0.75 | 93 | empty |
| 2 | 114 | 0.40 | 0.75 | 27 | SFG |
| 3 | 50 | 0.32 | 0.78 | 12 | empty |
| 4 | 80 | 0.32 | 0.73 | 23 | empty |
| 5 | 56 | 0.27 | 0.74 | 16 | SFG |
Interfaces
1 interface between chains.
- A–B · 490 Ų buried · 7 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 1AQJ · PDBe 1AQJ · UniProt P14385
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