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Structure of the GTP-binding protein TrmE from Thermotoga maritima complexed with 5-formyl-THF

Analyse Structure of the GTP-binding protein TrmE from Thermotoga maritima complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1XZQ
Type
protein
Length
566 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.9
Source
Thermotoga maritima
Molecule
Probable tRNA modification GTPase trmE
UniProt
Q9WYA4
Ligands
FON
Pockets
6 · best druggability 0.72

Structure

x-ray diffraction · resolution 2.9 · 2 distinct chains · 42% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProbable tRNA modification GTPase trmEprotein44947% helix, 17% strandQ9WYA4
BProbable tRNA modification GTPase trmEprotein11723% helix, 36% strandQ9WYA4

Ligands and binding sites

  • FON · N-{[4-({[(6R)-2-amino-5-formyl-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)phenyl]carbonyl}-L-glutamic acid · 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13770.720.8338FON
22420.630.8225FON
31890.500.7725empty
41210.420.7616empty
5830.400.7831empty

Interfaces

1 interface between chains.

  • A–B · 1511 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 1XZQ · Structure of the GTP-binding protein trme from thermotoga maritima complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WYA4 · AlphaFold monomer V2.0 prediction for tRNA modification GTPase mnme (Q9WYA4) · a predicted model of the same protein · chain B against A, TM-score 0.98

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