Research workbench
Structure of a O-methyltransferase from coxiella burnetii
Analyse Structure of a O-methyltransferase from coxiella burnetii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TR6
- Type
- protein
- Length
- 222 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- O-methyltransferase
- EC
- 2.1.1.-
- UniProt
- Q83D22
- Ligands
- SAH, NI
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-methyltransferase (EC 2.1.1.-) | protein | 222 | 46% helix, 20% strand | Q83D22 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.48 | 0.76 | 39 | NI, SAH |
| 2 | 51 | 0.38 | 0.81 | 16 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 3TR6 · Structure of a O-methyltransferase from Coxiella burnetii · the same entry in another collection · chain A against A, TM-score 1.00
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 Q83D22
- Elsewhere: RCSB PDB 3TR6 · PDBe 3TR6 · UniProt Q83D22
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