PDBsum entry 1qpw

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protein ligands Protein-protein interface(s) links
Oxygen transport PDB id
Protein chains
141 a.a. *
146 a.a. *
HEM ×2
Waters ×574
* Residue conservation analysis
PDB id:
Name: Oxygen transport
Title: Crystal structure determination of porcine hemoglobin at 1.8a resolution
Structure: Poricine hemoglobin (alpha subunit). Chain: a, c. Poricine hemoglobin (beta subunit). Chain: b, d
Source: Sus scrofa. Pig. Organism_taxid: 9823. Other_details: taiwanese pig from slaughterhouse. Other_details: taiwanese pig from slaughterhouse
Biol. unit: Tetramer (from PQS)
1.80Å     R-factor:   0.207     R-free:   0.251
Authors: T.-H.Lu,K.Panneerselvam,Y.-C.Liaw,P.Kan,C.-J.Lee
Key ref:
T.H.Lu et al. (2000). Structure determination of porcine haemoglobin. Acta Crystallogr D Biol Crystallogr, 56, 304-312. PubMed id: 10713517 DOI: 10.1107/S0907444900000093
30-May-99     Release date:   04-Jun-99    
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Protein chains
Pfam   ArchSchema ?
P01965  (HBA_PIG) -  Hemoglobin subunit alpha
141 a.a.
141 a.a.
Protein chains
Pfam   ArchSchema ?
P02067  (HBB_PIG) -  Hemoglobin subunit beta
147 a.a.
146 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     hemoglobin complex   1 term 
  Biological process     transport   2 terms 
  Biochemical function     protein binding     6 terms  


DOI no: 10.1107/S0907444900000093 Acta Crystallogr D Biol Crystallogr 56:304-312 (2000)
PubMed id: 10713517  
Structure determination of porcine haemoglobin.
T.H.Lu, K.Panneerselvam, Y.C.Liaw, P.Kan, C.J.Lee.
To investigate a potential candidate material for making artificial red blood cells to supplement blood transfusion, the X-ray structure of porcine haemoglobin at 1.8 A resolution was determined as part of research towards synthesizing human blood. Porcine haemoglobin was crystallized by the vapor-diffusion method, producing crystals of dimensions 0.3-0.5 mm after successive seeding. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 68.10, b = 72.27, c = 114.85 A. The initial phase was determined by the molecular-replacement method, using human oxyhaemoglobin as a model. The final R factor was 21.1% for 36 820 reflections after validation of 574 water molecules. The r.m.s. deviations of bond lengths, angles, torsion angles and improper angles from their ideal values are 0.017 A, 3.0, 20.6 and 1.8 degrees, respectively. The average B factor is 33.63 A(2) for the haemoglobin molecule and 50.53 A(2) for the water molecules. The structure could be superimposed on a 2.8 A resolution structure with an r.m.s. difference of 0.59 A in main-chain atomic positions and 1. 27 A in side-chain atomic positions. Porcine and human haemoglobins are compared. A tentative model for artificial blood is proposed based on the complementarity relationship of the surface charges between haemoglobin and the surrounding cell membrane.
  Selected figure(s)  
Figure 6.
Figure 6 (a) The haem group with proximal histidine (His87), distal histidine (His58) and surrounding residues up to a radius of 4.0 from the [1] subunit. (b) The heme group with proximal histidine (His92), distal histidine (His63) and surrounding residues up to a radius of 4.0 from the [1] subunit.
Figure 8.
Figure 8 The surface-charge distributions (using INSIGHTII) of (a) [1] subunit, with 180 rotation to show the complementarity to (b) [2] subunit.
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 304-312) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19191451 X.Hong, and Q.Hao (2009).
Measurements of accurate x-ray scattering data of protein solutions using small stationary sample cells.
  Rev Sci Instrum, 80, 014303.  
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