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Structure and mechanism of mRNA cap (guanine N-7) methyltransferase

Analyse Structure and mechanism of mRNA cap (guanine N-7) methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RI1
Type: protein
Length: 252 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MRNA capping enzyme
UniProt: Q8SR66
Ligands: SAH, GTG
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MRNA capping enzyme	protein	252	39% helix, 27% strand	Q8SR66

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · chains A
GTG · 7-methyl-guanosine-5'-triphosphate-5'-guanosine · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	455	0.66	0.78	43	SAH, GTG

Compared structures

1RI1 · Structure and mechanism of mRNA cap (guanine N-7) methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
Q8SR66 · AlphaFold monomer V2.0 prediction for mRNA cap guanine-N7 methyltransferase (Q8SR66) · 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 Q8SR66
Elsewhere: RCSB PDB 1RI1 · PDBe 1RI1 · UniProt Q8SR66

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