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Crystal structure of the methyltranferase domain of human HEN1 in complex with adomet

Analyse Crystal structure of the methyltranferase domain of human HEN1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WY0
Type: protein
Length: 199 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Small RNA 2'-O-methyltransferase
EC: 2.1.1.-
UniProt: Q5T8I9
Ligands: SAM
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Small RNA 2'-O-methyltransferase (EC 2.1.1.-)	protein	199	33% helix, 27% strand	Q5T8I9

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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	153	0.46	0.76	25	SAM
2	192	0.46	0.74	19	empty

Compared structures

5WY0 · Crystal structure of the methyltranferase domain of human HEN1 in complex with AdoMet · the same entry in another collection · chain A against A, TM-score 1.00
Q5T8I9 · AlphaFold monomer V2.0 prediction for small RNA 2'-O-methyltransferase (Q5T8I9) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q5T8I9
Elsewhere: RCSB PDB 5WY0 · PDBe 5WY0 · UniProt Q5T8I9

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