Research workbench
Histamine methyltransferase complexed with the antimalarial drug amodiaquine
Analyse Histamine methyltransferase complexed with the antimalarial drug amodiaquine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AOU
- Type
- protein
- Length
- 577 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
- CQA
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histamine N-methyltransferase (EC 2.1.1.8) | protein | 288 | 43% helix, 23% strand | P50135 |
| B | Histamine N-methyltransferase | protein | 289 | 44% helix, 23% strand | P50135 |
Ligands and binding sites
- CQA · 4-[(7-chloroquinolin-4-yl)amino]-2-[(diethylamino)methyl]phenol · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 565 | 0.78 | 0.84 | 65 | CQA |
| 2 | 671 | 0.78 | 0.83 | 66 | CQA |
| 3 | 571 | 0.68 | 0.78 | 62 | empty |
Interfaces
1 interface between chains.
- A–B · 415 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified, 1 d-amino (oxidation, D-amino acid).
Compared structures
- 2AOU · Histamine Methyltransferase Complexed with the Antimalarial Drug Amodiaquine · 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 2AOU · PDBe 2AOU · UniProt P50135
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