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Crystal structure of trmn from thermus thermophilus

Analyse Crystal structure of trmn from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TMA
Type: protein
Length: 332 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyltransferase
EC: 2.1.1.-
UniProt: Q72IH5
Ligands: PO4
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methyltransferase (EC 2.1.1.-)	protein	332	34% helix, 26% strand	Q72IH5

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

Pockets

4 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	196	0.55	0.79	29	empty
2	82	0.35	0.76	24	empty
3	51	0.28	0.75	13	empty
4	59	0.27	0.74	11	empty

Compared structures

3TMA · Crystal structure of TrmN from Thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
Q72IH5 · AlphaFold monomer V2.0 prediction for tRNA (GUANINE(6)-N2)-methyltransferase (Q72IH5) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q72IH5
Elsewhere: RCSB PDB 3TMA · PDBe 3TMA · UniProt Q72IH5

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