1qfc
From Proteopedia
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|PDB= 1qfc |SIZE=350|CAPTION= <scene name='initialview01'>1qfc</scene>, resolution 2.70Å | |PDB= 1qfc |SIZE=350|CAPTION= <scene name='initialview01'>1qfc</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfc OCA], [http://www.ebi.ac.uk/pdbsum/1qfc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qfc RCSB]</span> | ||
}} | }} | ||
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[[Category: Svensson, C.]] | [[Category: Svensson, C.]] | ||
[[Category: Uppenberg, J.]] | [[Category: Uppenberg, J.]] | ||
| - | [[Category: FE]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: PO4]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: metal phosphatase]] | [[Category: metal phosphatase]] | ||
| - | ''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 23:12:40 2008'' |
Revision as of 20:12, 30 March 2008
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Acid phosphatase, with EC number 3.1.3.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF RAT PURPLE ACID PHOSPHATASE
Overview
Tartrate-resistant acid phosphatase (TRAP) is a mammalian di-iron- containing enzyme that belongs to the family of purple acid phosphatases (PAP). It is highly expressed in a limited number of tissues, predominantly in bone-resorbing osteoclasts and in macrophages of spleen. We have determined the crystal structure of rat TRAP in complex with a phosphate ion to 2.7 A resolution. The fold resembles that of the catalytic domain of kidney bean purple acid phosphatase (KBPAP), although the sequence similarity is limited to the active site residues. A surface loop near the active site is absent due to proteolysis, leaving the active-site easily accessible from the surrounding solvent. This, we believe, gives a structural explanation for the observed proteolytic activation of TRAP. The current structure was determined at a relatively high pH and without any external reducing agents. It is likely that it represents an oxidized and therefore catalytically inactive form of the enzyme.
About this Structure
1QFC is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a mammalian purple acid phosphatase., Uppenberg J, Lindqvist F, Svensson C, Ek-Rylander B, Andersson G, J Mol Biol. 1999 Jul 2;290(1):201-11. PMID:10388567
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