Research workbench
Crystal structure of Y200L mutant of rat catechol-O-methyltransferase in complex with adomet and 3,5-dinitrocatechol
Analyse Crystal structure of Y200L mutant of rat catechol-O-methyltransferase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FHR
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catechol O-methyltransferase
- EC
- 2.1.1.6
- UniProt
- P22734
- Ligands
- DNC, SAM, MG, BR
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Catechol O-methyltransferase (EC 2.1.1.6) | protein | 213 | 47% helix, 20% strand | P22734 |
Ligands and binding sites
- DNC · 3,5-dinitrocatechol · ligand · 2 copies · chains A, B
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- BR · Bromide 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.67 | 0.86 | 35 | DNC, MG, SAM |
| 2 | 181 | 0.65 | 0.85 | 35 | DNC, MG, SAM |
| 3 | 251 | 0.53 | 0.76 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 2569 Ų buried · 75 hydrogen bonds · protein-protein
Compared structures
- 5FHR · Crystal structure of Y200L mutant of Rat Catechol-O-Methyltransferase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P22734 · AlphaFold monomer V2.0 prediction for catechol O-methyltransferase (P22734) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 5FHR · PDBe 5FHR · UniProt P22734
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