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Crystal structure of human METTL5-TRMT112 complex, the 18S rRNA M6A1832 methyltransferase at 1.6A resolution

Analyse Crystal structure of human METTL5-TRMT112 complex, the 18S rRNA M6A1832… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6H2U
Type: protein
Length: 321 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9NRN9, Q9UI30
Ligands: SO4

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	203	—	Q9NRN9
B	—	protein	118	—	Q9UI30

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A, B

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

Compared structures

6H2U · Crystal structure of human METTL5-TRMT112 complex, the 18S rRNA m6A1832 methyltransferase… · the same entry in another collection · chain B against B, TM-score 1.00
Q9NRN9 · AlphaFold monomer V2.0 prediction for rRNA N6-adenosine- methyltransferase METTL5 (Q9NRN9) · a predicted model of the same protein · chain A against A, TM-score 0.95
Q9UI30 · AlphaFold monomer V2.0 prediction for multifunctional methyltransferase subunit… · a predicted model of the same protein · chain B against A, TM-score 0.90

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 Q9NRN9
Every structure of UniProt Q9UI30
Elsewhere: RCSB PDB 6H2U · PDBe 6H2U · UniProt Q9NRN9 · UniProt Q9UI30

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