Research workbench
Structure analysis of entamoeba histolytica methyltransferase ehmeth
Analyse Structure analysis of entamoeba histolytica methyltransferase ehmeth in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QV2
- Type
- protein
- Length
- 320 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-cytosine DNA methyltransferase
- EC
- 2.1.1.37
- UniProt
- Q6Q386
- Ligands
- SAH, SO4
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-cytosine DNA methyltransferase (EC 2.1.1.37) | protein | 320 | 36% helix, 15% strand | Q6Q386 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 343 | 0.66 | 0.81 | 39 | SAH |
| 2 | 66 | 0.31 | 0.74 | 15 | empty |
Compared structures
- 3QV2 · Structure Analysis of Entamoeba histolytica methyltransferase EhMeth · 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 Q6Q386
- Elsewhere: RCSB PDB 3QV2 · PDBe 3QV2 · UniProt Q6Q386
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