1hml
From Proteopedia
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|PDB= 1hml |SIZE=350|CAPTION= <scene name='initialview01'>1hml</scene>, resolution 1.7Å | |PDB= 1hml |SIZE=350|CAPTION= <scene name='initialview01'>1hml</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Lactose_synthase Lactose synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.22 2.4.1.22] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lactose_synthase Lactose synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.22 2.4.1.22] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hml OCA], [http://www.ebi.ac.uk/pdbsum/1hml PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hml RCSB]</span> | ||
}} | }} | ||
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[[Category: Ren, J.]] | [[Category: Ren, J.]] | ||
[[Category: Stuart, D I.]] | [[Category: Stuart, D I.]] | ||
- | [[Category: CA]] | ||
- | [[Category: SO4]] | ||
- | [[Category: ZN]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:43 2008'' |
Revision as of 18:07, 30 March 2008
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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
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