Research workbench

Thermus thermophilus M5C1942 methyltransferase rlmo

Analyse Thermus thermophilus M5C1942 methyltransferase rlmo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DMG
Type: protein
Length: 770 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein TTHA1493
UniProt: Q5SI81
Ligands: SAM
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative uncharacterized protein TTHA1493	protein	385	32% helix, 30% strand	Q5SI81

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	962	0.77	0.79	81	SAM
2	780	0.76	0.80	71	SAM
3	572	0.68	0.78	75	empty
4	254	0.64	0.82	26	empty
5	57	0.34	0.78	15	empty

Interfaces

1 interface between chains.

A–B · 1788 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

4DMG · Thermus thermophilus m5C1942 methyltransferase RlmO · 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 Q5SI81
Elsewhere: RCSB PDB 4DMG · PDBe 4DMG · UniProt Q5SI81

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