Structure analysis

CRYSTAL STRUCTURE OF THE N-TERMINAL LAMININ G-LIKE DOMAIN OF SHBG IN COMPLEX WITH DIHYDROTESTOSTERONE

X-ray diffraction
1.55Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 15146.45 Å2
Buried surface area: 3156.79 Å2
Dissociation area: 733.07 Å2
Dissociation energy (ΔGdiss): -3.96 kcal/mol
Dissociation entropy (TΔSdiss): 12.09 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-137579
    Assembly 1
Confidence : 59%
No. subunits : 2
Symmetry : C2
3DComplex & QSbio predictionx
No. subunits : Unclear
Symmetry : Unclear
Evidence : This biological assembly agrees with the prediction of EPPIC but not of PISA

Macromolecules

Chain: A
Length: 170 amino acids
Theoretical weight: 18.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04278 (Residues: 42-217; Coverage: 46%)
Gene name: SHBG
Pfam: Laminin G domain
InterPro:
CATH: Jelly Rolls
SCOP: Laminin G-like module
PDBe-KB: UniProt Coverage View: P04278  
117020406080100120140160
 
50100150
UniProt
P04278
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces

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