› 2mf9

Solution NMR

Solution structure of the N-terminal domain of human FKBP38 (FKBP38NTD)

Released:
DOI: 10.2210/pdb2mf9/pdb
PDB entry 2mf9 coloured by chain, ensemble of 20 models, front view.
PDB entry 2mf9 coloured by chain, ensemble of 20 models, side view.
PDB entry 2mf9 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Functional role of the flexible N-terminal extension of FKBP38 in catalysis.
Kang C, Ye H, Chia J, Choi BH, Dhe-Paganon S, Simon B, Schütz U, Sattler M, Yoon HS
Sci Rep 3 2985 (2013)
PMID: 24145868

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP8 Chain: A
Molecule details ›
Chain: A
Length: 157 amino acids
Theoretical weight: 16.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14318 (Residues: 58-183, 184-205; Coverage: 36%)
Gene names: FKBP38, FKBP8
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 92%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

FK506-Binding Proteins and Their Diverse Functions.
Tong et al. (2015)
2 other articles

3 mentions without citation

Functional role of the flexible N-terminal extension of FKBP38 in catalysis.
Kang et al. (2013)
2 more