Structure analysis

The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog m5(11,8)-(E)-OH

X-ray diffraction
1.65Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 6529.01 Å2
Buried surface area: 816.44 Å2
Dissociation area: 408.22 Å2
Dissociation energy (ΔGdiss): -3.17 kcal/mol
Dissociation entropy (TΔSdiss): 5.55 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-171693
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 6754.04 Å2
Buried surface area: 857.83 Å2
Dissociation area: 428.92 Å2
Dissociation energy (ΔGdiss): -4.29 kcal/mol
Dissociation entropy (TΔSdiss): 5.56 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-171693

Macromolecules

Chains: A, B
Length: 128 amino acids
Theoretical weight: 14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q13451 (Residues: 16-140; Coverage: 27%)
Gene names: AIG6, FKBP5, FKBP51
Pfam: FKBP-type peptidyl-prolyl cis-trans isomerase
PDBe-KB: UniProt Coverage View: Q13451  
1128102030405060708090100110120
 
50100GAPATVTEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEIAHLLIKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGE
UniProt
Q13451
Chains
Flexibility predictions
Ligand binding sites
Sequence conservation

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