Structure analysis

Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative

X-ray diffraction
2.7Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 27660.06 Å2
Buried surface area: 8784.98 Å2
Dissociation area: 3,541.02 Å2
Dissociation energy (ΔGdiss): 29.89 kcal/mol
Dissociation entropy (TΔSdiss): 14.58 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-155932
Complex Portal ID: CPX-2165

Macromolecules

Chain: A
Length: 379 amino acids
Theoretical weight: 44.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49354 (Residues: 1-379; Coverage: 100%)
Gene name: FNTA
Pfam: Protein prenyltransferase alpha subunit repeat
InterPro: Protein prenyltransferase, alpha subunit
CATH: Protein prenylyltransferase
SCOP: Protein prenylyltransferase

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Chain: B
Length: 437 amino acids
Theoretical weight: 48.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49356 (Residues: 1-437; Coverage: 100%)
Gene name: FNTB
Pfam: Prenyltransferase and squalene oxidase repeat
InterPro:
CATH: Glycosyltransferase
SCOP: Protein prenyltransferases

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