Structure analysis

Crystal structure of hFA9 EGF repeat with O-glucose trisaccharide

X-ray diffraction
2.2Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 3543.95 Å2
Buried surface area: 1013.57 Å2
Dissociation area: 28.34 Å2
Dissociation energy (ΔGdiss): 4.46 kcal/mol
Dissociation entropy (TΔSdiss): 0.03 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133190
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 3393.48 Å2
Buried surface area: 904.97 Å2
Dissociation area: 177.87 Å2
Dissociation energy (ΔGdiss): -4.86 kcal/mol
Dissociation entropy (TΔSdiss): 1.74 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133190
Assembly 3 (preferred)
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Multimeric state: monomeric
Accessible surface area: 3285.32 Å2
Buried surface area: 1012.79 Å2
Dissociation area: 43.63 Å2
Dissociation energy (ΔGdiss): 12.36 kcal/mol
Dissociation entropy (TΔSdiss): 0.04 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133190

Macromolecules

Chains: A, B, C
Length: 50 amino acids
Theoretical weight: 5.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00740 (Residues: 92-130; Coverage: 9%)
Gene name: F9
Pfam: EGF-like domain
InterPro:
CATH: Laminin
PDBe-KB: UniProt Coverage View: P00740  
1505101520253035404550
 
2040MDIVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELLEHHHHHH
UniProt
P00740
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Sequence conservation

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