Research workbench
Histamine methyltransferase (natural variant I105) complexed with the acetylcholinesterase inhibitor and ALTZHEIMER'S disease drug tacrine
Analyse Histamine methyltransferase (natural variant I105) complexed with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AOW
- Type
- protein
- Length
- 576 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histamine N-methyltransferase
- EC
- 2.1.1.8
- UniProt
- P50135
- Ligands
- THA
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Histamine N-methyltransferase (EC 2.1.1.8) | protein | 288 | 45% helix, 22% strand | P50135 |
Ligands and binding sites
- THA · Tacrine · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 630 | 0.75 | 0.81 | 59 | THA |
| 2 | 653 | 0.73 | 0.80 | 59 | THA |
| 3 | 541 | 0.66 | 0.77 | 54 | empty |
| 4 | 59 | 0.46 | 0.84 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 332 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2AOW · Histamine Methyltransferase (Natural Variant I105) Complexed with the… · the same entry in another collection · chain A against A, TM-score 1.00
- P50135 · AlphaFold monomer V2.0 prediction for histamine N-methyltransferase (P50135) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P50135
- Elsewhere: RCSB PDB 2AOW · PDBe 2AOW · UniProt P50135
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