1zag
From Proteopedia
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|PDB= 1zag |SIZE=350|CAPTION= <scene name='initialview01'>1zag</scene>, resolution 2.80Å | |PDB= 1zag |SIZE=350|CAPTION= <scene name='initialview01'>1zag</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zag OCA], [http://www.ebi.ac.uk/pdbsum/1zag PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zag RCSB]</span> | ||
}} | }} | ||
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[[Category: Chirino, A J.]] | [[Category: Chirino, A J.]] | ||
[[Category: Sanchez, L M.]] | [[Category: Sanchez, L M.]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: NDG]] | ||
[[Category: lipid mobilization factor]] | [[Category: lipid mobilization factor]] | ||
[[Category: secreted mhc class i homolog]] | [[Category: secreted mhc class i homolog]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:33:05 2008'' |
Revision as of 22:33, 30 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN ZINC-ALPHA-2-GLYCOPROTEIN
Overview
Zn-alpha2-glycoprotein (ZAG) is a soluble protein that is present in serum and other body fluids. ZAG stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. The 2.8 angstrom crystal structure of ZAG resembles a class I major histocompatibility complex (MHC) heavy chain, but ZAG does not bind the class I light chain beta2-microglobulin. The ZAG structure includes a large groove analogous to class I MHC peptide binding grooves. Instead of a peptide, the ZAG groove contains a nonpeptidic compound that may be implicated in lipid catabolism under normal or pathological conditions.
About this Structure
1ZAG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules., Sanchez LM, Chirino AJ, Bjorkman P, Science. 1999 Mar 19;283(5409):1914-9. PMID:10206894
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