Research workbench
Crystal structure of the catalytic domain of METTL3/METTL14 complex with sah
Analyse Crystal structure of the catalytic domain of METTL3/METTL14 complex with sah in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5K7W
- Type
- protein
- Length
- 489 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N6-adenosine-methyltransferase 70 kda subunit; N6-adenosine-methyltransferase subunit…
- EC
- 2.1.1.62
- UniProt
- Q86U44, Q9HCE5
- Ligands
- SAH
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N6-adenosine-methyltransferase 70 kda subunit (EC 2.1.1.62) | protein | 205 | 22% helix, 28% strand | Q86U44 |
| B | N6-adenosine-methyltransferase subunit METTL14 (EC 2.1.1.62) | protein | 284 | 30% helix, 22% strand | Q9HCE5 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.69 | 0.84 | 45 | empty |
| 2 | 540 | 0.68 | 0.78 | 67 | SAH |
| 3 | 62 | 0.38 | 0.79 | 13 | empty |
| 4 | 68 | 0.37 | 0.78 | 15 | empty |
| 5 | 58 | 0.30 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2514 Ų buried · 46 hydrogen bonds · protein-protein
Compared structures
- 5K7W · Crystal structure of the catalytic domain of Mettl3/Mettl14 complex with SAH · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HCE5 · AlphaFold monomer V2.0 prediction for N6-adenosine-methyltransferase non-catalytic… · a predicted model of the same protein · chain B 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 0.99
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
- Every structure of UniProt Q9HCE5
- Elsewhere: RCSB PDB 5K7W · PDBe 5K7W · UniProt Q86U44 · UniProt Q9HCE5
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