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1hml
From Proteopedia
| 1hml, resolution 1.70Å () | |||||||||
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| Ligands: | , , | ||||||||
| Activity: | Lactose synthase, with EC number 2.4.1.22 | ||||||||
| Domains: | LYZ1 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1HML is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Ren J, Stuart DI, Acharya KR. Alpha-lactalbumin possesses a distinct zinc binding site. J Biol Chem. 1993 Sep 15;268(26):19292-8. PMID:8366079
Page seeded by OCA on Tue Feb 17 04:04:42 2009
