Structure analysis

Complex of the FimH lectin with a C-linked naphtyl alpha-D-mannoside in soaked trigonal crystals at 2.40 A resolution

X-ray diffraction
2.4Å resolution
Source organism: Escherichia coli UTI89
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 7524.66 Å2
Buried surface area: 103.62 Å2
Dissociation area: 51.81 Å2
Dissociation energy (ΔGdiss): 7.76 kcal/mol
Dissociation entropy (TΔSdiss): -0.13 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140004
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 7447.11 Å2
Buried surface area: 107.82 Å2
Dissociation area: 53.91 Å2
Dissociation energy (ΔGdiss): 7.5 kcal/mol
Dissociation entropy (TΔSdiss): -0.13 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140004

Macromolecules

Chains: A, B
Length: 158 amino acids
Theoretical weight: 16.92 KDa
Source organism: Escherichia coli UTI89
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08191 (Residues: 22-179; Coverage: 57%)
Gene names: JW4283, b4320, fimH
Pfam: FimH, mannose binding
InterPro:
CATH: Fimbrial-type adhesion domain
PDBe-KB: UniProt Coverage View: P08191  
115820406080100120140
 
50100150
UniProt
P08191
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Sequence conservation

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