Structure analysis

Neisseria DNA mimic protein DMP12

X-ray diffraction
1.85Å resolution
Source organism: Neisseria meningitidis MC58
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 6409.03 Å2
Buried surface area: 84.1 Å2
Dissociation area: 42.05 Å2
Dissociation energy (ΔGdiss): 6.18 kcal/mol
Dissociation entropy (TΔSdiss): -1.47 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-191671
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 6237.8 Å2
Buried surface area: 82.33 Å2
Dissociation area: 41.16 Å2
Dissociation energy (ΔGdiss): 6.17 kcal/mol
Dissociation entropy (TΔSdiss): -1.47 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-191671
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 10922.91 Å2
Buried surface area: 1890.35 Å2
Dissociation area: 861.96 Å2
Dissociation energy (ΔGdiss): 1.56 kcal/mol
Dissociation entropy (TΔSdiss): 11.43 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-191672

Macromolecules

Chains: A, B
Length: 119 amino acids
Theoretical weight: 14.07 KDa
Source organism: Neisseria meningitidis MC58
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JXC6 (Residues: 1-118; Coverage: 100%)
Gene name: NMB2123
Pfam: DNA-mimic protein
InterPro:
CATH: Hypothetical protein yfbM fold

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