5EO6

Coproporphyrinogen III oxidase (HemF) from Acinetobacter baumannii


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.45 Å
  • R-Value Free: 0.168 
  • R-Value Work: 0.135 
  • R-Value Observed: 0.136 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure of oproporphyrinogen III oxidase (aerobic) from Acinetobacter baumannii

Abendroth, J.Mayclin, S.J.Lorimer, D.D.Edwards, T.E.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Coproporphyrinogen oxidase
A, B
324Acinetobacter baumanniiMutation(s): 0 
Gene Names: hemFABUW_0377ACX61_01995AKG96_15100
EC: 1.3.3.3
UniProt
Find proteins for A0A0D5YE19 (Acinetobacter baumannii)
Explore A0A0D5YE19 
Go to UniProtKB:  A0A0D5YE19
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0D5YE19
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 71.14α = 90
b = 97.16β = 115.79
c = 71.26γ = 90
Software Package:
Software NamePurpose
XDSdata reduction
XSCALEdata scaling
MOLREPphasing
PHENIXrefinement
ARPmodel building
Cootmodel building
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-12-02
    Type: Initial release
  • Version 1.1: 2023-09-27
    Changes: Data collection, Database references, Derived calculations, Refinement description