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Crystal structure of mRNA cap guanine-N7 methyltransferase obtained by limited proteolysis

Analyse Crystal structure of mRNA cap guanine-N7 methyltransferase obtained by limited… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5E9W
Type
protein
Length
1,093 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MRNA cap guanine-N7 methyltransferase
EC
2.1.1.56
UniProt
O43148
Ligands
SAH
Pockets
6 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 41% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CMRNA cap guanine-N7 methyltransferase (EC 2.1.1.56)protein27341% helix, 26% strandO43148
BMRNA cap guanine-N7 methyltransferase (EC 2.1.1.56)protein27341% helix, 25% strandO43148
DMRNA cap guanine-N7 methyltransferase (EC 2.1.1.56)protein27441% helix, 25% strandO43148

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18400.750.7957SAH
211240.710.7585SAH
34400.640.7745SAH
44000.620.7744SAH
51930.500.7735empty

Interfaces

2 interfaces between chains.

  • B–D · 298 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 227 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5E9W · Crystal structure of mRNA cap guanine-N7 methyltransferase obtained by limited proteolysis · the same entry in another collection · chain D against D, 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 C against A, TM-score 0.99

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