1fjm
From Proteopedia
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|PDB= 1fjm |SIZE=350|CAPTION= <scene name='initialview01'>1fjm</scene>, resolution 2.1Å | |PDB= 1fjm |SIZE=350|CAPTION= <scene name='initialview01'>1fjm</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACB:3-METHYL-ASPARTIC+ACID'>ACB</scene>, <scene name='pdbligand=ADD:2,6,8-TRIMETHYL-3-AMINO-9-BENZYL-9-METHOXYNONANOIC+ACID'>ADD</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CAB:4-CARBOXY-4-AMINOBUTANAL'>CAB</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DAM:N-METHYL-ALPHA-BETA-DEHYDROALANINE'>DAM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjm OCA], [http://www.ebi.ac.uk/pdbsum/1fjm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fjm RCSB]</span> | ||
}} | }} | ||
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[[Category: Kuriyan, J.]] | [[Category: Kuriyan, J.]] | ||
[[Category: Nairn, A C.]] | [[Category: Nairn, A C.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: MN]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''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 20:24:10 2008'' |
Revision as of 17:24, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Activity: | Phosphoprotein phosphatase, with EC number 3.1.3.16 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PROTEIN SERINE/THREONINE PHOSPHATASE-1 (ALPHA ISOFORM, TYPE I) COMPLEXED WITH MICROCYSTIN-LR TOXIN
Overview
The crystal structure of mammalian protein phosphatase-1, complexed with the toxin microcystin and determined at 2.1 A resolution, reveals that it is a metalloenzyme unrelated in architecture to the tyrosine phosphatases. Two metal ions are positioned by a central beta-alpha-beta-alpha-beta scaffold at the active site, from which emanate three surface grooves that are potential binding sites for substrates and inhibitors. The carboxy terminus is positioned at the end of one of the grooves such that regulatory sequences following the domain might modulate function. The fold of the catalytic domain is expected to be closely preserved in protein phosphatases 2A and 2B (calcineurin).
About this Structure
1FJM is a Single protein structure of sequence from Microcystis aeruginosa and Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1., Goldberg J, Huang HB, Kwon YG, Greengard P, Nairn AC, Kuriyan J, Nature. 1995 Aug 31;376(6543):745-53. PMID:7651533
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