MolNFT v1 · #9172 · protein
Crystal structure of human pnmt complexed with SK&F 29661 and ADOHCY(SAH)
1HNN · Phenylethanolamine N-methyltransferase: “Crystal structure of human pnmt complexed with SK&F 29661 and ADOHCY(SAH)”. X-ray diffraction, 2 ligands (SAH, SKF), 6 pockets (best druggability 0.82). MolNFT v1 #9172 on GenesisL1: 3D…
- PDB
- 1HNN
- 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, SKF
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylethanolamine N-methyltransferase (EC 2.1.1.28) | protein | 261 | 37% 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
- SKF · 1,2,3,4-tetrahydro-isoquinoline-7-sulfonic acid amide · 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.82 | 0.96 | 43 | SAH, SKF |
| 2 | 129 | 0.76 | 0.94 | 30 | SAH |
| 3 | 74 | 0.74 | 0.97 | 18 | SKF |
| 4 | 232 | 0.56 | 0.78 | 42 | empty |
| 5 | 54 | 0.47 | 0.85 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 559 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1HNN · Crystal structure of human pnmt complexed with SK&F 29661 and ADOHCY(SAH) · 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 1HNN · PDBe 1HNN · UniProt P11086
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