1OUU

CARBONMONOXY TROUT HEMOGLOBIN I

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.286 
  • R-Value Work: 0.162 

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This is version 1.4 of the entry. See complete history. 


Literature

The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms.

Tame, J.R., Wilson, J.C., Weber, R.E.

(1996) J Mol Biol 259: 749-760

  • DOI: https://doi.org/10.1006/jmbi.1996.0355
  • Primary Citation of Related Structures:  
    1OUT, 1OUU

  • PubMed Abstract: 

    We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 angstroms and 2.5 angstroms, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions.

    • Organizational Affiliation: 

    Department of Chemistry, University of York, Helsington, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HEMOGLOBIN I
A, C
143Oncorhynchus mykissMutation(s): 0 
UniProt
Find proteins for P02019 (Oncorhynchus mykiss)
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Go to UniProtKB:  P02019
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UniProt GroupP02019
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  • Reference Sequence
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(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
HEMOGLOBIN I
B, D
146Oncorhynchus mykissMutation(s): 0 
UniProt
Find proteins for P02142 (Oncorhynchus mykiss)
Explore P02142 
Go to UniProtKB:  P02142
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02142
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.286 
  • R-Value Work: 0.162 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 65.2α = 90
b = 79.8β = 90
c = 122.9γ = 90
Software Package:
Software NamePurpose
PROLSQrefinement
XDSdata reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-01-11
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-06-05
    Changes: Data collection, Database references, Derived calculations, Other
  • Version 1.4: 2024-10-23
    Changes: Structure summary