Structure analysis

Crystal Structure of Human GRP CRD

X-ray diffraction
1.9Å resolution
Source organism: Homo sapiens
Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo tetramer
Accessible surface area: 25633.88 Å2
Buried surface area: 4629.54 Å2
Dissociation area: 274.3 Å2
Dissociation energy (ΔGdiss): -9.51 kcal/mol
Dissociation entropy (TΔSdiss): 13.1 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-174905
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 13059.94 Å2
Buried surface area: 1894.57 Å2
Dissociation area: 477.58 Å2
Dissociation energy (ΔGdiss): 10.42 kcal/mol
Dissociation entropy (TΔSdiss): 11.46 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-174904
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 13122.53 Å2
Buried surface area: 2186.37 Å2
Dissociation area: 479.41 Å2
Dissociation energy (ΔGdiss): 10.4 kcal/mol
Dissociation entropy (TΔSdiss): 11.47 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-174904

Macromolecules

Chains: A, B, C, D
Length: 144 amino acids
Theoretical weight: 16.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q3ZCW2 (Residues: 38-172; Coverage: 79%)
Gene names: GRP, HSPC159, LGALSL
Pfam: Galactoside-binding lectin
InterPro:
CATH: Jelly Rolls

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