6HRK | pdb_00006hrk

Structure of a far-red fluorescent biliprotein derived from a far-red induced allophycocyanin F subunit from a thermophilic cyanobacterium Chroococcidiopsis thermalis

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.52 Å
  • R-Value Free: 
    0.332 (Depositor), 0.290 (DCC) 
  • R-Value Work: 
    0.274 (Depositor), 0.240 (DCC) 
  • R-Value Observed: 
    0.277 (Depositor) 

Starting Model: experimental
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Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted BLAClick on this verticalbar to view details

This is version 1.3 of the entry. See complete history. 


Literature

Control of a far-red/near-infrared spectral switch in an artificial fluorescent biliprotein derived from allophycocyanin

Hou, Y.N., Hoppner, A., Rao, A.G., Lahav, Y., Kumar Das, P., Ding, W.L., Jiang, X.X., Hu, J.L., Schapiro, I., Noy, D., Zhao, K.H.

(2022) Protein Sci 31


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Allophycocyanin beta-18 subunit apoprotein
A, B, C, D
147Chroococcidiopsis thermalis PCC 7203Mutation(s): 18 
Gene Names: Chro_1766
UniProt
Find proteins for K9TY40 (Chroococcidiopsis thermalis (strain PCC 7203))
Explore K9TY40 
Go to UniProtKB:  K9TY40
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupK9TY40
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.52 Å
  • R-Value Free:  0.332 (Depositor), 0.290 (DCC) 
  • R-Value Work:  0.274 (Depositor), 0.240 (DCC) 
  • R-Value Observed: 0.277 (Depositor) 
Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 61.248α = 90
b = 74.823β = 90.67
c = 61.031γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
xia2data reduction
autoPROCdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted BLAClick on this verticalbar to view details

View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-10-09
    Type: Initial release
  • Version 1.1: 2022-10-26
    Changes: Database references, Refinement description
  • Version 1.2: 2024-01-31
    Changes: Data collection, Refinement description
  • Version 1.3: 2024-11-20
    Changes: Structure summary