1R9H

Structural Genomics of C.elegans: FKBP-type Peptidylprolyl Isomerase

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.210 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history. 


Literature

Structural Genomics of C.elegans: FKBP-type Peptidylprolyl Isomerase

Li, S., Finley, J., Luan, C.-H., Qiu, S., Gray, R., Shang, Q., Luo, D., Hongli, C., Zhao, J., Huang, W.-Y., DeLucas, L.J., Nagy, L., Stanton, A., Luo, M., Symersky, J., Schormann, N., Lin, G., Tsao, J., Johnson, D.H., Carson, W.M.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FK506 Binding protein family135Caenorhabditis elegansMutation(s): 0 
Gene Names: f31d4.3
UniProt
Find proteins for O45418 (Caenorhabditis elegans)
Explore O45418 
Go to UniProtKB:  O45418
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO45418
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.210 
  • R-Value Observed: 0.210 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.417α = 90
b = 52.417β = 90
c = 210.8γ = 120
Software Package:
Software NamePurpose
CNSrefinement

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-12-02
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-24
    Changes: Structure summary
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references