MolNFT v1 · #8457 · protein
Catechol O-methyltransferase
1H1D · Catechol-O-methyltransferase: “Catechol O-methyltransferase”. X-ray diffraction, 3 ligands (SAM, BIA, MG), 1 pocket (best druggability 0.63). MolNFT v1 #8457 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1H1D
- Type
- protein
- Length
- 213 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
- P22734
- Ligands
- SAM, BIA, MG
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catechol-O-methyltransferase (EC 2.1.1.6) | protein | 213 | 47% helix, 20% strand | P22734 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
- BIA · 1-(3,4,dihydroxy-5-nitrophenyl)-3-{4-[3-(trifluoromethyl) phenyl] piperazin-1-yl}propan-1-one · ligand · chains A
- MG · Magnesium ion · metal · 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 | 153 | 0.63 | 0.85 | 32 | SAM, BIA |
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 P22734
- Elsewhere: RCSB PDB 1H1D · PDBe 1H1D · UniProt P22734
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