Research workbench

Crystal structure of a tRNA (guanine-N1)-methyltransferase from acinetobacter baumannii

Analyse Crystal structure of a tRNA (guanine-N1)-methyltransferase from acinetobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MYQ
Type: protein
Length: 458 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TRNA (guanine-N(1)-)-methyltransferase
EC: 2.1.1.228
UniProt: A0A0D5YDX5
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	TRNA (guanine-N(1)-)-methyltransferase (EC 2.1.1.228)	protein	229	42% helix, 18% strand	A0A0D5YDX5
B	TRNA (guanine-N(1)-)-methyltransferase (EC 2.1.1.228)	protein	229	45% helix, 18% strand	A0A0D5YDX5

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	407	0.70	0.82	47	empty
2	473	0.69	0.80	58	empty
3	169	0.51	0.78	27	empty

Interfaces

1 interface between chains.

A–B · 3295 Å² buried · 61 hydrogen bonds · protein-protein

Compared structures

7MYQ · Crystal structure of a tRNA (guanine-N1)-methyltransferase from Acinetobacter baumannii · the same entry in another collection · chain B against B, 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 A0A0D5YDX5
Elsewhere: RCSB PDB 7MYQ · PDBe 7MYQ · UniProt A0A0D5YDX5

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.