MolNFT v1 · #103139 · protein
Mouse apo-comt
4P7F · Catechol O-methyltransferase: “Mouse apo-comt”. X-ray diffraction, 3 ligands (NA, PO4, PI), 1 pocket (best druggability 0.58). MolNFT v1 #103139 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4P7F
- 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
- O88587
- Ligands
- NA, PO4, PI
- Pockets
- 1 · best druggability 0.58
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 | O88587 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- PO4 · Phosphate ion · ion · 4 copies · chains A
- PI · Hydrogenphosphate ion · ion · 2 copies · 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 | 217 | 0.58 | 0.80 | 28 | PI |
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 4P7F · PDBe 4P7F · UniProt O88587
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