Research workbench
The structure of phenylethanolamine N-methyltransferase in complex with S-adenosylhomocysteine and an iodinated inhibitor
Analyse The structure of phenylethanolamine N-methyltransferase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N7J
- Type
- protein
- Length
- 528 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylethanolamine N-methyltransferase
- EC
- 2.1.1.28
- UniProt
- P11086
- Ligands
- SAH, IDI
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylethanolamine N-methyltransferase (EC 2.1.1.28) | protein | 261 | 36% helix, 25% strand | P11086 |
| B | Phenylethanolamine N-methyltransferase (EC 2.1.1.28) | protein | 267 | 38% helix, 25% strand | P11086 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
- IDI · 7-iodo-1,2,3,4-tetrahydro-isoquinoline · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.82 | 0.96 | 40 | SAH, IDI |
| 2 | 122 | 0.75 | 0.94 | 28 | SAH |
| 3 | 76 | 0.74 | 0.97 | 18 | IDI |
| 4 | 147 | 0.49 | 0.78 | 21 | empty |
| 5 | 127 | 0.45 | 0.77 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 477 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1N7J · The structure of Phenylethanolamine N-methyltransferase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P11086 · AlphaFold monomer V2.0 prediction for phenylethanolamine N-methyltransferase (P11086) · 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 P11086
- Elsewhere: RCSB PDB 1N7J · PDBe 1N7J · UniProt P11086
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.