2q5e
From Proteopedia
| Line 3: | Line 3: | ||
{{Structure | {{Structure | ||
|PDB= 2q5e |SIZE=350|CAPTION= <scene name='initialview01'>2q5e</scene>, resolution 2.510Å | |PDB= 2q5e |SIZE=350|CAPTION= <scene name='initialview01'>2q5e</scene>, resolution 2.510Å | ||
| - | |SITE= | + | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+1'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+1'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Residue+C+1'>AC3</scene>, <scene name='pdbsite=AC4:Mg+Binding+Site+For+Residue+D+1'>AC4</scene>, <scene name='pdbsite=AC5:Mg+Binding+Site+For+Residue+E+1'>AC5</scene>, <scene name='pdbsite=AC6:Mg+Binding+Site+For+Residue+F+1'>AC6</scene>, <scene name='pdbsite=AC7:Mg+Binding+Site+For+Residue+G+1'>AC7</scene> and <scene name='pdbsite=AC8:Mg+Binding+Site+For+Residue+H+1'>AC8</scene> |
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|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> | |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> | ||
| Line 13: | Line 13: | ||
'''Crystal structure of human carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2''' | '''Crystal structure of human carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2''' | ||
| + | |||
| + | ==Overview== | ||
| + | The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases. | ||
==About this Structure== | ==About this Structure== | ||
2Q5E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q5E OCA]. | 2Q5E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q5E OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | Structural genomics of protein phosphatases., Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK, J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18058037 18058037] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Phosphoprotein phosphatase]] | [[Category: Phosphoprotein phosphatase]] | ||
| Line 37: | Line 43: | ||
[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 10:02:25 2008'' |
Revision as of 08:02, 26 March 2008
| |||||||
| , resolution 2.510Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | CTDSP2, NIF2, OS4 (Homo sapiens) | ||||||
| Activity: | Phosphoprotein phosphatase, with EC number 3.1.3.16 | ||||||
| Domains: | NIF | ||||||
| Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
Overview
The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptional regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases.
About this Structure
2Q5E is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural genomics of protein phosphatases., Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK, J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:18058037
Page seeded by OCA on Wed Mar 26 10:02:25 2008
Categories: Homo sapiens | Phosphoprotein phosphatase | Single protein | Almo, S C. | Bain, K T. | Bonanno, J B. | Burley, S K. | Dickey, M. | Lau, C. | NYSGXRC, New York Structural GenomiX Research Consortium. | Romero, R. | Sauder, J M. | Smith, D. | Wasserman, S. | Hydrolase | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi-2 | Structural genomic
