Structure analysis

Structure of the carbohydrate-recognition domain of the C-type lectin mincle bound to trehalose

X-ray diffraction
1.4Å resolution
Source organism: Bos taurus
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 6796.27 Å2
Buried surface area: 927.16 Å2
Dissociation area: 256.07 Å2
Dissociation energy (ΔGdiss): 0.77 kcal/mol
Dissociation entropy (TΔSdiss): 4.17 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-122748
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 6778.72 Å2
Buried surface area: 173.49 Å2
Dissociation area: 43.34 Å2
Dissociation energy (ΔGdiss): 11.69 kcal/mol
Dissociation entropy (TΔSdiss): 0.04 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-122748

Macromolecules

Chains: A, B
Length: 134 amino acids
Theoretical weight: 15.74 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E1BHM0 (Residues: 79-211; Coverage: 63%)
Gene name: CLEC4E
Pfam: Lectin C-type domain
InterPro:
CATH: Mannose-Binding Protein A, subunit A
PDBe-KB: UniProt Coverage View: E1BHM0  
1134102030405060708090100110120130
 
50100ACPLKWFHFQSSCYLFSPDTMSWRASLKNCSSMGAHLVVINTQEEQEFLYYTKPRKKEFYIGLTDQVTEGQWQWVDGTPFTKSLSFWDAGEPNNLVTVEDCATIRDSSNPRQNWNDVPCFFNMFRVCEMPERKI
UniProt
E1BHM0
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Sequence conservation

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