Alpha-lactalbumin

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</StructureSection>
</StructureSection>
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== 3D Structures of α-lactalbumin ==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*α-lactalbumin
 
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**[[1alc]] – LCA – baboon
 
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**[[1hml]], [[1b9o]], [[3b0i]], [[3b0o]] – hLCA –human
 
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**[[1a4v]] – hLCA Ca-binding domain<br />
 
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**[[1cb3]] – hLCA residues 1-13 - NMR<br />
 
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**[[1hfx]] – LCA – guinea pig
 
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**[[1hfy]], [[3b0k]] – gLCA – goat
 
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**[[1hmk]], [[1fkq]], [[1fkv]] – gLCA (mutant)
 
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**[[1f6r]], [[1f6s]], [[2g4n]], [[6ip9]] – bLCA - bovine
 
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**[[1hfz]] – bLCA (mutant)
 
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*α-LCA complexes
 
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**[[1nf5]] – mLCA + β-1,4-galactosyl transferase + glucose – mouse
 
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**[[1nhe]] – mLCA + β-1,4-galactosyl transferase + UDP
 
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**[[1nkh]] – mLCA + β-1,4-galactosyl transferase + UDP + Mn
 
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**[[1nmm]] – mLCA + β-1,4-galactosyl transferase (mutant)
 
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**[[1nqi]] - mLCA + β-1,4-galactosyl transferase
 
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**[[1nwg]] - mLCA + β-1,4-galactosyl transferase + butanoyl-glucosamine
 
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**[[1o23]] - mLCA + β-1,4-galactosyl transferase + UDP-glucose
 
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**[[1oqm]] - mLCA + β-1,4-galactosyl transferase + UDP-acetyl-galactosamine
 
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**[[1pzy]] - mLCA (mutant) + β-1,4-galactosyl transferase + acetyl-glucosamine + UDP + Mn
 
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**[[1yro]] - mLCA + β-1,4-galactosyl transferase + UDP-galactose + Mn
 
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**[[1fyc]] - mLCA (mutant) + β-1,4-galactosyl transferase + UDP-galactose + Ca
 
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**[[2fyd]], [[2fyc]] - mLCA (mutant) + β-1,4-galactosyl transferase + glucose + UDP-acetylgalactosamine + Mn<br />
 
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**[[4l41]] - hLCA + β-1,4-galactosyl transferase (mutant)<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 10:40, 4 March 2019

Human α-lactalbumin complex with sulfate, Zn+2 (grey) and Ca+2 (green) ions (PDB code 1hml).

Drag the structure with the mouse to rotate

References

  1. ↑ Permyakov EA, Berliner LJ. alpha-Lactalbumin: structure and function. FEBS Lett. 2000 May 19;473(3):269-74. PMID:10818224

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky

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