1N5U

X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH HEME


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.235 

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This is version 1.2 of the entry. See complete history


Literature

The Atomic Structure of Human Methemalbumin at 1.9 A

Wardell, M.Wang, Z.Ho, J.X.Robert, J.Ruker, F.Ruble, J.Carter, D.C.

(2002) Biochem Biophys Res Commun 291: 813-819

  • DOI: https://doi.org/10.1006/bbrc.2002.6540
  • Primary Citation of Related Structures:  
    1N5U

  • PubMed Abstract: 

    The high resolution structure of hemalbumin was determined by single crystal X-ray diffraction to a resolution of 1.9 A. The structure revealed the protoporphyrin IX bound to a single site within a hydrophobic cavity in subdomain IB, one of the principal binding sites for long chain fatty acid. The iron is penta coordinated with the fifth ligand comprised of the hydroxyl oxygen of Tyr-161 (phenolic oxygen to heme plane distance: 2.73 A) in an otherwise completely hydrophobic pocket. The heme propionic acid residues form salt bridges with His-142 and Lys-190, which together with a series of hydrophobic interactions, enclose and secure the heme within the IB helical motif. A detailed discussion of the structure together with its implications for the development of potential blood substitutes is presented.


  • Organizational Affiliation

    New Century Pharmaceuticals, Inc., 895 Martin Road, Huntsville, Alabama 35824, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SERUM ALBUMIN585Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P02768 (Homo sapiens)
Explore P02768 
Go to UniProtKB:  P02768
PHAROS:  P02768
GTEx:  ENSG00000163631 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02768
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.235 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 183.116α = 90
b = 37.909β = 105.04
c = 94.832γ = 90
Software Package:
Software NamePurpose
MERLOTphasing
CNXrefinement

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-06-24
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance