Sandbox Reserved 1698
From Proteopedia
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== Important amino acids== | == Important amino acids== | ||
| - | This is diagram of the <scene name='89/892741/Electron_active_site/1'>active site</scene> in the 1INP. | + | This is diagram of the <scene name='89/892741/Electron_active_site/1'>active site</scene>in the 1INP. |
| + | <ref> PMID:33172890</ref> | ||
Electron density attribute to substrate binding. Two calcium ions (CA1 and CA2). The three metal sites in the active site of 1INP show Mg2+, Ca2+. Mg2+ in metal site are seem in the ligand interactions in both 1INP. This magnesium ions stabilize the protein and ligand to be able to catalyze the substrate. | Electron density attribute to substrate binding. Two calcium ions (CA1 and CA2). The three metal sites in the active site of 1INP show Mg2+, Ca2+. Mg2+ in metal site are seem in the ligand interactions in both 1INP. This magnesium ions stabilize the protein and ligand to be able to catalyze the substrate. | ||
== Structural highlights == | == Structural highlights == | ||
| - | Our protein | + | Our protein has secondary structure contains <scene name='89/892741/77_helix/1'>77% alpha</scene>, and <scene name='89/892741/Beta_sheets_33/2'>33% beta sheets |
</scene> | </scene> | ||
| - | + | Also contains <scene name='89/892741/Tertiary_structure/1'>tertiary structure</scene> which is formed by the hydrophobic and non polar | |
| + | |||
Not able to see the active site due too <scene name='89/892741/Space_filing/1'>space filling</scene> | Not able to see the active site due too <scene name='89/892741/Space_filing/1'>space filling</scene> | ||
== Other important features == | == Other important features == | ||
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Included catalytic amino acids are Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313. This all the protein contributed to hydrogen bonding to the ligand. | Included catalytic amino acids are Thr 312, Lys 270, Ser 268, Glu 269, Ser 157, Asp 156, Thr 158, Ala 291, Lys 294, and Thr 313. This all the protein contributed to hydrogen bonding to the ligand. | ||
| + | "DPIDxT" six-amino acid motif anchor metal binding. sites likely involve catalysis | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Current revision
| This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699. |
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1INP
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Dollins DE, Xiong JP, Endo-Streeter S, Anderson DE, Bansal VS, Ponder JW, Ren Y, York JD. A Structural Basis for Lithium and Substrate Binding of an Inositide Phosphatase. J Biol Chem. 2020 Nov 10. pii: RA120.014057. doi: 10.1074/jbc.RA120.014057. PMID:33172890 doi:http://dx.doi.org/10.1074/jbc.RA120.014057
