6JKQ

Crystal structure of aspartate transcarbamoylase from Trypanosoma cruzi (Ligand-free form)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.81 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.178 
  • R-Value Observed: 0.182 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history. 


Literature

Crystallographic snapshots of Trypanosoma cruzi aspartate transcarbamoylase revealed an ordered Bi-Bi reaction mechanism

Matoba, K., Shiba, T., Nara, T., Aoki, T., Nagasaki, S., Hayamizu, R., Honma, T., Tanaka, A., Inoue, M., Matsuoka, S., Balogun, E.O., Inaoka, D.K., Kita, K., Harada, S.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Aspartate carbamoyltransferase
A, B, C, D, E
A, B, C, D, E, F
327Trypanosoma cruziMutation(s): 0 
Gene Names: C3747_31g124
EC: 2.1.3.2
UniProt
Find proteins for O15636 (Trypanosoma cruzi)
Explore O15636 
Go to UniProtKB:  O15636
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO15636
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.81 Å
  • R-Value Free: 0.265 
  • R-Value Work: 0.178 
  • R-Value Observed: 0.182 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 78.419α = 69.56
b = 79.282β = 82.9
c = 92.016γ = 63.25
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2020-03-04
    Type: Initial release
  • Version 1.1: 2023-11-22
    Changes: Data collection, Database references, Refinement description