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Crystal Structure of the AQP1 water channel
1J4N
Primary Citation

Structural basis of water-specific transport through the AQP1 water channel.

Sui, H.,  Han, B.G.,  Lee, J.K.,  Walian, P.,  Jap, B.K.

Journal: (2001) Nature 414: 872-878

PubMed: 11780053  
DOI: 10.1038/414872a  
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PubMed Abstract:
Water channels facilitate the rapid transport of water across cell membranes in response to osmotic gradients. These channels are believed to be involved in many physiological processes that include renal water conservation, neuro-homeostasis, digestion, regulation of body temperature and reproduction.... [ Read More & Search PubMed Abstracts ]
 
  •   Molecular Description Hide
    Classification: Membrane Protein
    Structure Weight: 29743.79
    Molecule: AQUAPORIN 1
    Polymer: 1 Type: protein Length: 271
    Chains: A
    Organism Bos taurus
    Gene Name AQP1
    UniProtKB:   Protein Feature View | Search PDB | P47865  
    P47865Molec. ProcessingAquaporin-1MotifCyHelicalExtrHelicCiHeCHelicalExtraceHeliCytHeliciHelExtHeliCytoplasmicPUP SitesUniProtKBSCOP domainsAquaporin-like PDB SitesSecstruc1J4N.APDBTooltip
     
  •   Source Hide
    Polymer: 1
    Scientific Name: Bos taurus   Taxonomy   Common Name: Cattle  
     
  •   Related PDB Entries Hide
    Identifier Details
    1FQY  Aquaporin-1 (1FQY) is a similar protein solved by EM. 
     
  •   Ligand Chemical Component Hide
    Identifier Formula Name Interactions
    BNG
    Search 
    Download      		BNG C15 H30 O6
    B-NONYLGLUCOSIDE
     
  •   External Domain Annotations Hide
     
  •   Structural Biology Knowledgebase Data Hide

    Information from the Structural Biology Knowledgebase  

     
 
Data in orange boxes are gathered from external resources (when available).
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  Biological Assembly 1       
Biological assembly 1 assigned by authors and generated by PISA,PQS (software)
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  •   Deposition Summary Hide
    Authors:   Sui, H.,  Han, B.-G.,  Lee, J.K.,  Walian, P.,  Jap, B.K.

    Deposition:   2001-10-19
    Release:   2002-03-27
    Last Modified (REVDAT):   2011-07-13
     
  •   Revision History    Hide
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    2011-07-13
    Version format compliance
    2011-07-13
    Biological assembly
     
  •   Experimental Details Hide
    Method:   X-RAY DIFFRACTION
    Exp. Data:
    N/A
    Resolution[Å]:   2.20
    R-Value: 0.266 (work)
    R-Free: 0.308
    Space Group: I 4 2 2
    Unit Cell:
      Length [Å] Angles [°]
    a = 93.33 α = 90.00 
    b = 93.33 β = 90.00 
    c = 180.49 γ = 90.00