Structure analysis

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

X-ray diffraction
2.9Å resolution
Source organism: Thermotoga maritima
Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 25600 Å2
Buried surface area: 5000 Å2
Dissociation area: 2,000 Å2
Dissociation energy (ΔGdiss): 14 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): -21 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: hetero tetramer
Accessible surface area: 49200 Å2
Buried surface area: 12100 Å2
Dissociation area: 1,000 Å2
Dissociation energy (ΔGdiss): 3 kcal/mol
Dissociation entropy (TΔSdiss): 15 kcal/mol
Interface energy (ΔGint): -58 kcal/mol
Symmetry number: 2

Macromolecules

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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
Pfam: GTP-binding protein TrmE N-terminus
InterPro:
CATH: Probable tRNA modification gtpase trme; domain 1
SCOP: TrmE formyl-THF-binding domain

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