1VJU

Coproporphyrinogen III oxidase from Leishmania major


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.180 
  • R-Value Work: 0.151 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Coproporphyrinogen III oxidase from Leishmania major

Structural Genomics of Pathogenic Protozoa Consortium

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Coproporphyrinogen III oxidase
A, B
309Leishmania majorMutation(s): 0 
EC: 1.3.3.3
UniProt
Find proteins for P84155 (Leishmania major)
Explore P84155 
Go to UniProtKB:  P84155
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP84155
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.180 
  • R-Value Work: 0.151 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.649α = 86.456
b = 53.734β = 77.126
c = 66.627γ = 61.501
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing
SHELXphasing
RESOLVEphasing
REFMACrefinement
SHELXDphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-04-13
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-04
    Changes: Refinement description
  • Version 1.4: 2018-01-31
    Changes: Database references
  • Version 1.5: 2023-12-27
    Changes: Data collection, Database references, Derived calculations