4NNR

FKBP13-FK506 Complex

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.98 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.159 
  • R-Value Observed: 0.159 

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This is version 1.1 of the entry. See complete history. 


Literature

Atomic structure of the Immunophilin FKBP13-FK506 Complex: Insights into the Composite Binding Surface for Calcineurin

Schultz, L.W., Martin, P.K., Liang, J., Schreiber, S.L., Clardy, J.

(1994) J Am Chem Soc 116: 3129-3130


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Peptidyl-prolyl cis-trans isomerase FKBP2
A, B
142Homo sapiensMutation(s): 0 
Gene Names: FKBP2, FKBP13
EC: 5.2.1.8
UniProt & NIH Common Fund Data Resources
Find proteins for P26885 (Homo sapiens)
Explore P26885 
Go to UniProtKB:  P26885
PHAROS:  P26885
GTEx:  ENSG00000173486 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP26885
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.98 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.159 
  • R-Value Observed: 0.159 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 74.26α = 90
b = 74.06β = 90
c = 39.24γ = 90
Software Package:
Software NamePurpose
SDMSdata collection
X-PLORmodel building
X-PLORrefinement
SDMSdata reduction
SCALEPACKdata scaling
X-PLORphasing

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-02-05
    Type: Initial release
  • Version 1.1: 2019-11-13
    Changes: Database references