5ZUT | pdb_00005zut

Crystal Structure of Yeast PCNA in Complex with N24 Peptide

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.82 Å
  • R-Value Free: 
    0.397 (Depositor), 0.370 (DCC) 
  • R-Value Work: 
    0.326 (Depositor), 0.320 (DCC) 
  • R-Value Observed: 
    0.330 (Depositor) 

Starting Models: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Crystal Structure of Yeast PCNA in Complex with N24 Peptide

Cheng, X.Y., Kuang, X.L., Zhou, Y., Xia, X.M., SU, Z.D.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Proliferating cell nuclear antigen289Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: POL30, YBR088C, YBR0811
UniProt
Find proteins for P15873 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P15873 
Go to UniProtKB:  P15873
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15873
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
N24B [auth E]18Homo sapiensMutation(s): 0 
Gene Names: PIK3R3
UniProt & NIH Common Fund Data Resources
Find proteins for Q5T4P3 (Homo sapiens)
Explore Q5T4P3 
Go to UniProtKB:  Q5T4P3
GTEx:  ENSG00000117461 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5T4P3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.82 Å
  • R-Value Free:  0.397 (Depositor), 0.370 (DCC) 
  • R-Value Work:  0.326 (Depositor), 0.320 (DCC) 
  • R-Value Observed: 0.330 (Depositor) 
Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 80.35α = 90
b = 84.03β = 93.62
c = 58.15γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data collection
PDB_EXTRACTdata extraction
XDSdata reduction
Aimlessdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2018-05-30
    Type: Initial release
  • Version 1.1: 2023-11-22
    Changes: Data collection, Database references, Refinement description
  • Version 1.2: 2024-06-05
    Changes: Data collection