Structure analysis

STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES: NRDD IN COMPLEX WITH DGTP

X-ray diffraction
2.45Å resolution
Source organism: Escherichia virus T4
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: 41622.54 Å2
Buried surface area: 9047.56 Å2
Dissociation area: 3,271.45 Å2
Dissociation energy (ΔGdiss): 30.75 kcal/mol
Dissociation entropy (TΔSdiss): 15.46 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-139363

Macromolecules

Chain: A
Length: 605 amino acids
Theoretical weight: 68.06 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P07071 (Residues: 1-605; Coverage: 100%)
Gene names: 49.1, 55.11/55.13, SUNY, nrdD
Pfam: Glycine radical
InterPro:
CATH: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain
SCOP: Class III anaerobic ribonucleotide reductase NRDD subunit

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