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Crystal structure of the archaeal tRNA M2G/M22G10 methyltransferase (ATRM11) in complex with S-adenosyl-L-methionine (SAM) from thermococcus kodakarensis

Analyse Crystal structure of the archaeal tRNA M2G/M22G10 methyltransferase (ATRM11) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5E72
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N2, N2-dimethylguanosine tRNA methyltransferase
UniProt: Q5JID5
Ligands: SAM
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N2, N2-dimethylguanosine tRNA methyltransferase	protein	323	34% helix, 32% strand	Q5JID5

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

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	128	0.49	0.79	29	SAM

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5E72 · Crystal structure of the archaeal tRNA m2G/m22G10 methyltransferase (aTrm11) in complex… · the same entry in another collection · chain A against A, TM-score 1.00

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 Q5JID5
Elsewhere: RCSB PDB 5E72 · PDBe 5E72 · UniProt Q5JID5

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