4ODC

Crystal structure of Trematomus bernacchii hemoglobin in a partially cyanided state

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.54 Å
  • R-Value Free: 0.197 
  • R-Value Work: 0.165 
  • R-Value Observed: 0.165 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history. 


Literature

Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin

Mazzarella, L., Merlino, A., Vitagliano, L., Verde, C., di Prisco, G., Peisach, J., Vergara, A.

(2014) RSC Adv 4: 25852-25856


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hemoglobin subunit alpha143Trematomus bernacchiiMutation(s): 1 
UniProt
Find proteins for P80043 (Trematomus bernacchii)
Explore P80043 
Go to UniProtKB:  P80043
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP80043
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Hemoglobin subunit beta146Trematomus bernacchiiMutation(s): 0 
UniProt
Find proteins for P80044 (Trematomus bernacchii)
Explore P80044 
Go to UniProtKB:  P80044
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP80044
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.54 Å
  • R-Value Free: 0.197 
  • R-Value Work: 0.165 
  • R-Value Observed: 0.165 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 86.88α = 90
b = 87.88β = 99.66
c = 55.25γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
SHELXSphasing
SHELXL-97refinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-12-24
    Type: Initial release
  • Version 1.1: 2019-12-11
    Changes: Advisory, Database references, Derived calculations
  • Version 1.2: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description