Structure analysis

Crystal structure of ADP, AMP, and FMN bound TM379

X-ray diffraction
2.8Å resolution
Source organism: Thermotoga maritima
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 27500 Å2
Buried surface area: 5600 Å2
Dissociation area: 800 Å2
Dissociation energy (ΔGdiss): -11 kcal/mol
Dissociation entropy (TΔSdiss): 13 kcal/mol
Interface energy (ΔGint): -17 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B
Length: 293 amino acids
Theoretical weight: 33.67 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9WZW1 (Residues: 1-293; Coverage: 100%)
Gene name: TM_0857
Pfam:
InterPro:
CATH:
SCOP:

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