MolNFT v1 · #11562 · protein
Crystal structure analysis of human histamine methyltransferase (ILE105 polymorphic variant) complexed with adohcy and antimalarial drug quinacrine
1JQE · Histamine N-methyltransferase: “Crystal structure analysis of human histamine methyltransferase (ILE105 polymorphic variant) complexed with…”. X-ray diffraction, 3 ligands (SAH, QUN, UNX), 4 pockets (best druggability 0.75). MolNFT…
- PDB
- 1JQE
- Type
- protein
- Length
- 560 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
- SAH, QUN, UNX
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Histamine N-methyltransferase (EC 2.1.1.8) | protein | 280 | 44% helix, 23% strand | P50135 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
- QUN · Quinacrine · ligand · chains A
- UNX · Unknown atom or ion · ion · 7 copies · chains 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 | 519 | 0.75 | 0.83 | 56 | SAH, QUN |
| 2 | 573 | 0.72 | 0.80 | 60 | SAH, UNX |
| 3 | 500 | 0.65 | 0.77 | 60 | empty |
| 4 | 57 | 0.39 | 0.80 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 432 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1JQE · Crystal Structure Analysis of Human Histamine Methyltransferase (Ile105 Polymorphic… · 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 B 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 1JQE · PDBe 1JQE · UniProt P50135
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