Structure analysis

Crystal structure of human calprotectin(S100A8/S100A9)

X-ray diffraction
1.8Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero tetramer
Accessible surface area: 17248.48 Å2
Buried surface area: 8961.33 Å2
Dissociation area: 4,056.87 Å2
Dissociation energy (ΔGdiss): 58.85 kcal/mol
Dissociation entropy (TΔSdiss): 34.53 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-138505
Complex Portal ID: CPX-37
Assembly 2 (preferred)
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Multimeric state: hetero tetramer
Accessible surface area: 17280.04 Å2
Buried surface area: 9105.75 Å2
Dissociation area: 1,286.07 Å2
Dissociation energy (ΔGdiss): 12.4 kcal/mol
Dissociation entropy (TΔSdiss): 12.71 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-138505
Complex Portal ID: CPX-37
Assembly 3
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Multimeric state: hetero tetramer
Accessible surface area: 17372.01 Å2
Buried surface area: 9121.79 Å2
Dissociation area: 4,175.92 Å2
Dissociation energy (ΔGdiss): 56.48 kcal/mol
Dissociation entropy (TΔSdiss): 34.65 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-138505
Complex Portal ID: CPX-37

Macromolecules

Chains: A, B, E, F, I, J
Length: 93 amino acids
Theoretical weight: 10.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05109 (Residues: 1-93; Coverage: 100%)
Gene names: CAGA, CFAG, MRP8, S100A8
Pfam: S-100/ICaBP type calcium binding domain
InterPro:
CATH: EF-hand
SCOP: S100 proteins

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Chains: C, D, G, H, K, L
Length: 113 amino acids
Theoretical weight: 13.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06702 (Residues: 2-114; Coverage: 99%)
Gene names: CAGB, CFAG, MRP14, S100A9
Pfam: S-100/ICaBP type calcium binding domain
InterPro:
CATH: EF-hand
SCOP: S100 proteins

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