1hml
From Proteopedia
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, resolution 1.7Å | |||||||
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Ligands: | , , | ||||||
Activity: | Lactose synthase, with EC number 2.4.1.22 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE
Overview
It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. However, the high resolution x-ray crystal structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A resolution (pH 7.6) does not reveal any significant change in conformation from the native state. The Zn2+ ion binds specifically in the "cleft" of alpha-lactalbumin (the region which forms the active site of the homologous protein lysozyme). This may suggest a possible role for Zn2+ binding in lactose synthase complex. The coordination of the Zn2+ ion involves a symmetry-related molecule in the crystal, the crystal contacts being stabilized by a SO4(2-) ion bound at the interface between three molecules.
About this Structure
1HML is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Alpha-lactalbumin possesses a distinct zinc binding site., Ren J, Stuart DI, Acharya KR, J Biol Chem. 1993 Sep 15;268(26):19292-8. PMID:8366079
Page seeded by OCA on Sun Mar 30 21:07:43 2008