5RPJ

PanDDA analysis group deposition -- Proteinase K changed state model for fragment Frag Xtal Screen B12a


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.27 Å
  • R-Value Free: 0.176 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.160 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 2.1 of the entry. See complete history


Literature

FragMAXapp: crystallographic fragment-screening data-analysis and project-management system.

Lima, G.M.A.Jagudin, E.Talibov, V.O.Benz, L.S.Marullo, C.Barthel, T.Wollenhaupt, J.Weiss, M.S.Mueller, U.

(2021) Acta Crystallogr D Struct Biol 77: 799-808

  • DOI: https://doi.org/10.1107/S2059798321003818
  • Primary Citation of Related Structures:  
    5ROC, 5ROD, 5ROE, 5ROF, 5ROG, 5ROH, 5ROI, 5ROJ, 5ROK, 5ROL, 5ROM, 5RON, 5ROO, 5ROP, 5ROQ, 5ROR, 5ROS, 5ROT, 5ROU, 5ROV, 5ROW, 5ROX, 5ROY, 5ROZ, 5RP0, 5RP1, 5RP2, 5RP3, 5RP4, 5RP5, 5RP6, 5RP7, 5RP8, 5RP9, 5RPA, 5RPB, 5RPC, 5RPD, 5RPE, 5RPF, 5RPG, 5RPH, 5RPI, 5RPJ, 5RPK, 5RPL, 5RPM, 5RPN, 5RPO, 5RPP

  • PubMed Abstract: 

    Crystallographic fragment screening (CFS) has become one of the major techniques for screening compounds in the early stages of drug-discovery projects. Following the advances in automation and throughput at modern macromolecular crystallography beamlines, the bottleneck for CFS has shifted from collecting data to organizing and handling the analysis of such projects. The complexity that emerges from the use of multiple methods for processing and refinement and to search for ligands requires an equally sophisticated solution to summarize the output, allowing researchers to focus on the scientific questions instead of on software technicalities. FragMAXapp is the fragment-screening project-management tool designed to handle CFS projects at MAX IV Laboratory. It benefits from the powerful computing infrastructure of large-scale facilities and, as a web application, it is accessible from everywhere.


  • Organizational Affiliation

    BioMAX, MAX IV Laboratory, Fotongatan 2, 224 84 Lund, Sweden.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Proteinase K279Parengyodontium albumMutation(s): 0 
Gene Names: PROK
EC: 3.4.21.64
UniProt
Find proteins for P06873 (Parengyodontium album)
Explore P06873 
Go to UniProtKB:  P06873
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06873
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.27 Å
  • R-Value Free: 0.176 
  • R-Value Work: 0.160 
  • R-Value Observed: 0.160 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 67.74α = 90
b = 67.74β = 90
c = 101.58γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
Aimlessdata scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Swedish Research CouncilSweden2018-06454

Revision History  (Full details and data files)

  • Version 1.0: 2021-05-26
    Type: Initial release
  • Version 2.0: 2021-06-23
    Changes: Atomic model, Data collection, Database references
  • Version 2.1: 2024-11-13
    Changes: Data collection, Database references, Structure summary