MolNFT v1 · #53081 · protein
Structure of the O-methyltransferase novp
2WK1: “Structure of the O-methyltransferase novp”. X-ray diffraction, 2 ligands (SAH, SO4), 1 pocket (best druggability 0.69). MolNFT v1 #53081 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2WK1
- Type
- protein
- Length
- 242 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Novp
- EC
- 2.1.1.-
- UniProt
- Q9L9F2
- Ligands
- SAH, SO4
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Novp (EC 2.1.1.-) | protein | 242 | 42% helix, 16% strand | Q9L9F2 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.69 | 0.84 | 46 | SAH |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 Q9L9F2
- Elsewhere: RCSB PDB 2WK1 · PDBe 2WK1 · UniProt Q9L9F2
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