Structure analysis

Structure of the p22phox A200G mutant in complex with p47phox peptide

X-ray diffraction
2.5Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 7922.35 Å2
Buried surface area: 1409.46 Å2
Dissociation area: 704.73 Å2
Dissociation energy (ΔGdiss): 5.28 kcal/mol
Dissociation entropy (TΔSdiss): 7.49 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-146610

Macromolecules

Chain: D
Length: 18 amino acids
Theoretical weight: 1.93 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P13498 (Residues: 151-168; Coverage: 9%)
Gene name: CYBA
PDBe-KB: UniProt Coverage View: P13498  
11824681012141618
 
51015PPSNPPPRPPAEARKKPS
UniProt
P13498
Chains
Flexibility predictions
Interaction interfaces

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Chain: A
Length: 131 amino acids
Theoretical weight: 14.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14598 (Residues: 156-285; Coverage: 33%)
Gene names: NCF1, NOXO2, SH3PXD1A
Pfam: SH3 domain
InterPro:
PDBe-KB: UniProt Coverage View: P14598  
1131102030405060708090100110120130
 
50100
UniProt
P14598
Chains
Domains
Secondary structure
Flexibility predictions
Interaction interfaces
Sequence conservation

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