Research workbench
Rat catechol O-methyltransferase in complex with N-[2-[2-(6- aminopurin-9-YL)ETHOXY]ETHYL]-5-(4-fluorophenyl)-2,3- dihydroxybenzamide at 1.91A
Analyse Rat catechol O-methyltransferase in complex with N-[2-[2-(6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5P9A
- 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
- 77N, D1D, MG, K
- Pockets
- 1 · best druggability 0.56
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 | 213 | 47% helix, 23% strand | P22734 |
Ligands and binding sites
- 77N · N-[2-[2-(6-aminopurin-9-yl)ethoxy]ethyl]-5-(4-fluorophenyl)-2,3-dihydroxybenzamide · ligand · chains A
- D1D · (4S,5S)-1,2-dithiane-4,5-diol · ligand · chains A
- MG · Magnesium ion · metal · chains A
- K · Potassium 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 | 152 | 0.56 | 0.82 | 27 | 77N |
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 5P9A · PDBe 5P9A · UniProt P22734
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