Research workbench
human COMT, double domain swap
Analyse human COMT, double domain swap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PYK
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.22
- Source
- Homo sapiens
- 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 · resolution 2.22 · 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
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