9L91 | pdb_00009l91

The crystal structure of human RyR3 Repeat12 domain in complex with Azumolene and AMP-PCP


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 
    0.317 (Depositor), 0.310 (DCC) 
  • R-Value Work: 
    0.268 (Depositor), 0.261 (DCC) 
  • R-Value Observed: 
    0.281 (Depositor) 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.0 of the entry. See complete history


Literature

Structural Basis for the Modulation of Ryanodine Receptor by Dantrolene and Azumolene

Hadiatullah, H.Lin, L.Yuchi, Z.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ryanodine receptor 3A [auth B],
B [auth A],
C,
D
218Homo sapiensMutation(s): 0 
Gene Names: RYR3HBRR
UniProt & NIH Common Fund Data Resources
Find proteins for Q15413 (Homo sapiens)
Explore Q15413 
Go to UniProtKB:  Q15413
PHAROS:  Q15413
GTEx:  ENSG00000198838 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ15413
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free:  0.317 (Depositor), 0.310 (DCC) 
  • R-Value Work:  0.268 (Depositor), 0.261 (DCC) 
  • R-Value Observed: 0.281 (Depositor) 
Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 261.666α = 90
b = 59.96β = 90
c = 60.759γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
Aimlessdata scaling
HKL-2000data reduction
PHENIXphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Not funded--

Revision History  (Full details and data files)

  • Version 1.0: 2025-10-22
    Type: Initial release