Research workbench
Zinc finger domain of METTL3-METTL14 N6-methyladenosine methyltransferase
Analyse Zinc finger domain of METTL3-METTL14 N6-methyladenosine methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YZ9
- Type
- protein
- Length
- 99 residues
- Chains
- 1
- Method
- solution nmr; solution scattering
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N6-adenosine-methyltransferase catalytic subunit
- EC
- 2.1.1.62
- UniProt
- Q86U44
- Ligands
- ZN
Structure
solution nmr; solution scattering · 1 distinct chain · 19% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N6-adenosine-methyltransferase catalytic subunit (EC 2.1.1.62) | protein | 99 | 19% helix, 6% strand | Q86U44 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YZ9 · zinc finger domain of METTL3-METTL14 N6-methyladenosine methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
- Q86U44 · AlphaFold monomer V2.0 prediction for N6-adenosine-methyltransferase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.29
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 Q86U44
- Elsewhere: RCSB PDB 5YZ9 · PDBe 5YZ9 · UniProt Q86U44
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.