Research workbench
Tetrahydroprotoberberine N-methyltransferase in complex with S- adenosylhomocysteine
Analyse Tetrahydroprotoberberine N-methyltransferase in complex with S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P3M
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetrahydroprotoberberine N-methyltransferase
- EC
- 2.1.1.122
- Ligands
- SAH, SO4
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetrahydroprotoberberine N-methyltransferase (EC 2.1.1.122) | protein | 336 | 49% helix, 16% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 757 | 0.76 | 0.80 | 66 | SAH |
| 2 | 77 | 0.39 | 0.78 | 16 | empty |
| 3 | 83 | 0.36 | 0.76 | 16 | empty |
Compared structures
- 6P3M · Tetrahydroprotoberberine N-methyltransferase in complex with S-adenosylhomocysteine · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6P3M · PDBe 6P3M
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