› 1bl4

X-ray diffraction
1.9Å resolution

FKBP MUTANT F36V COMPLEXED WITH REMODELED SYNTHETIC LIGAND

Released:
DOI: 10.2210/pdb1bl4/pdb
PDB entry 1bl4 coloured by chain, front view.
PDB entry 1bl4 coloured by chain, side view.
PDB entry 1bl4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Redesigning an FKBP-ligand interface to generate chemical dimerizers with novel specificity.
Clackson T, Yang W, Rozamus LW, Hatada M, Amara JF, Rollins CT, Stevenson LF, Magari SR, Wood SA, Courage NL, Lu X, Cerasoli F, Gilman M, Holt DA
Proc Natl Acad Sci U S A 95 10437-42 (1998)
PMID: 9724721

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158814 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1A Chains: A, B
Molecule details ›
Chains: A, B
Length: 107 amino acids
Theoretical weight: 11.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62942 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP1, FKBP12, FKBP1A
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:
Ligand AP1 2 x AP1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 32.73Å b: 41.85Å c: 43.59Å
α: 62.61° β: 82.75° γ: 85.29°
R-values:
R R work R free
0.188 0.188 0.23
Expression system: Escherichia coli

Quick links

Citations

70 review citations

Adoptive T cell therapy for cancer in the clinic.
June CH. (2007)
69 more

8 mentions without citation

Redesigning an FKBP-ligand interface to generate chemical dimerizers with novel specificity.
Clackson et al. (1998)
7 more