Structure analysis

A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE

X-ray diffraction
1.9Å resolution
Source organism: Escherichia coli
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: homo dimer
Accessible surface area: 19278.98 Å2
Buried surface area: 1515.84 Å2
Dissociation area: 540.09 Å2
Dissociation energy (ΔGdiss): -10.71 kcal/mol
Dissociation entropy (TΔSdiss): 12.49 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-139986

Macromolecules

Chain: A
Length: 212 amino acids
Theoretical weight: 23.21 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08179 (Residues: 1-212; Coverage: 100%)
Gene names: JW2485, b2500, purN
Pfam: Formyl transferase
InterPro:
CATH: Formyl transferase, N-terminal domain
SCOP: Formyltransferase

Search similar proteins