MolNFT v1 · #104030 · protein
Human comt, double domain swap
4PYK · Catechol O-methyltransferase: “Human comt, double domain swap”. X-ray diffraction, 3 ligands (NA, MG, CL), 3 pockets (best druggability 0.70). MolNFT v1 #104030 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4PYK
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catechol O-methyltransferase
- EC
- 2.1.1.6
- UniProt
- P21964
- Ligands
- NA, MG, CL
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catechol O-methyltransferase (EC 2.1.1.6) | protein | 214 | 51% helix, 14% strand | P21964 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 365 | 0.70 | 0.82 | 39 | empty |
| 2 | 163 | 0.53 | 0.79 | 29 | CL |
| 3 | 63 | 0.34 | 0.76 | 12 | empty |
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 P21964
- Elsewhere: RCSB PDB 4PYK · PDBe 4PYK · UniProt P21964
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.