1xzq

X-ray diffraction
2.9Å resolution

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

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
tRNA modification GTPase MnmE Chain: A
Molecule details ›
Chain: A
Length: 482 amino acids
Theoretical weight: 54.19 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYA4 (Residues: 1-450; Coverage: 100%)
Gene names: TM_0267, mnmE, trmE
Sequence domains:
Structure domains:
tRNA modification GTPase MnmE Chain: B
Molecule details ›
Chain: B
Length: 149 amino acids
Theoretical weight: 16.36 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYA4 (Residues: 1-117; Coverage: 26%)
Gene names: TM_0267, mnmE, trmE
Sequence domains: GTP-binding protein TrmE N-terminus
Structure domains: Probable tRNA modification gtpase trme; domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P62
Unit cell:
a: 130.03Å b: 130.03Å c: 113.84Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.256 0.25 0.307
Expression system: Escherichia coli