MolNFT v1 · #103072 · protein
Crystal structure of mouse comt bound to an inhibitor
4P58 · Catechol O-methyltransferase: “Crystal structure of mouse comt bound to an inhibitor”. X-ray diffraction, 1 ligand (2F6), 2 pockets (best druggability 0.52). MolNFT v1 #103072 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4P58
- Type
- protein
- Length
- 205 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
- O88587
- Ligands
- 2F6
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catechol O-methyltransferase (EC 2.1.1.6) | protein | 205 | 47% helix, 23% strand | O88587 |
Ligands and binding sites
- 2F6 · 1',3'-dimethyl-1H,1'H-3,4'-bipyrazole · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.52 | 0.88 | 17 | 2F6 |
| 2 | 144 | 0.45 | 0.76 | 21 | 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 O88587
- Elsewhere: RCSB PDB 4P58 · PDBe 4P58 · UniProt O88587
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