Research workbench
Crystal structure of the human METTL3-METTL14 complex bound to SAM
Analyse Crystal structure of the human METTL3-METTL14 complex bound to SAM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L6E
- Type
- protein
- Length
- 435 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
- SAM, MG
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N6-adenosine-methyltransferase 70 kda subunit (EC 2.1.1.62) | protein | 199 | 24% helix, 28% strand | Q86U44 |
| B | N6-adenosine-methyltransferase subunit METTL14 (EC 2.1.1.62) | protein | 236 | 28% helix, 25% strand | Q9HCE5 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
- MG · Magnesium ion · metal · chains A
- ACT · Acetate ion · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.62 | 0.78 | 39 | empty |
| 2 | 285 | 0.59 | 0.78 | 53 | SAM |
| 3 | 51 | 0.41 | 0.82 | 17 | empty |
| 4 | 76 | 0.34 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2058 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5L6E · Crystal structure of the human METTL3-METTL14 complex bound to SAM · 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 0.99
- 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 0.96
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 5L6E · PDBe 5L6E · UniProt Q86U44 · UniProt Q9HCE5
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