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The structure of the rRNA methyltransferase ermc': implications for the reaction mechanism

Analyse The structure of the rRNA methyltransferase ermc': implications for the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QAO
Type: protein
Length: 236 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ermc' methyltransferase
EC: 2.1.1.48
UniProt: P13956
Ligands: SAM
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ermc' methyltransferase (EC 2.1.1.48)	protein	236	42% helix, 19% strand	P13956

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	226	0.68	0.85	38	SAM
2	100	0.41	0.77	13	empty

Compared structures

1QAO · The structure of the rRNA methyltransferase ermc': implications for the reaction mechanism · the same entry in another collection · chain A against A, TM-score 1.00
P13956 · AlphaFold monomer V2.0 prediction for rRNA adenine N-6-methyltransferase (P13956) · 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 P13956
Elsewhere: RCSB PDB 1QAO · PDBe 1QAO · UniProt P13956

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