7Q32

Mutant D24G of uridine phosphorylase from E. coli


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.154 

Starting Model: experimental
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This is version 1.2 of the entry. See complete history


Literature

Mutant D24G of uridine phosphorylase from E. coli

Polyakov, K.Safonova, T.Antipov, A.Okorokova, N.Mordkovich, N.Veiko, V.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Uridine phosphorylaseA [auth AAA],
B [auth BBB]
250Escherichia coli K-12Mutation(s): 1 
Gene Names: udpb3831JW3808
EC: 2.4.2.3
UniProt
Find proteins for P12758 (Escherichia coli (strain K12))
Explore P12758 
Go to UniProtKB:  P12758
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP12758
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.202 
  • R-Value Work: 0.154 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 150.07α = 90
b = 150.07β = 90
c = 46.36γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Not fundedRussian Federation--

Revision History  (Full details and data files)

  • Version 1.0: 2022-05-04
    Type: Initial release
  • Version 1.1: 2022-05-11
    Changes: Database references, Structure summary
  • Version 1.2: 2024-01-31
    Changes: Data collection, Derived calculations, Refinement description