MolNFT v1 · #117484 · protein
Crystal structure of the mRNA cap guanine-N7 methyltransferase - modular lobe (416-456) deletion
5E9J · MRNA cap guanine-N7 METHYLTRANSFERASE,MRNA cap guanine-N7…: “Crystal structure of the mRNA cap guanine-N7 methyltransferase - modular lobe (416-456) deletion”. X-ray diffraction, 1 ligand (SAH), 5 pockets (best druggability 0.69).…
- PDB
- 5E9J
- Type
- protein
- Length
- 548 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MRNA cap guanine-N7 METHYLTRANSFERASE,MRNA cap guanine-N7 methyltransferase
- EC
- 2.1.1.56
- UniProt
- O43148
- Ligands
- SAH
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | MRNA cap guanine-N7 METHYLTRANSFERASE,MRNA cap guanine-N7 methyltransferase (EC 2.1.1.56) | protein | 274 | 39% helix, 26% strand | O43148 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 551 | 0.69 | 0.78 | 46 | SAH |
| 2 | 563 | 0.67 | 0.77 | 49 | SAH |
| 3 | 358 | 0.63 | 0.78 | 45 | empty |
| 4 | 114 | 0.40 | 0.75 | 16 | empty |
| 5 | 68 | 0.33 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 546 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5E9J · Crystal structure of the mRNA cap guanine-N7 methyltransferase - modular lobe (416-456)… · the same entry in another collection · chain A against A, TM-score 1.00
- O43148 · AlphaFold monomer V2.0 prediction for mRNA cap guanine-N7 methyltransferase (O43148) · a predicted model of the same protein · chain B 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 O43148
- Elsewhere: RCSB PDB 5E9J · PDBe 5E9J · UniProt O43148
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