Ann Taylor sandbox 120
From Proteopedia
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==Trypsin bound to an inhibitor== | ==Trypsin bound to an inhibitor== | ||
| - | Trypsin is a serine protease. It works with a catalytic triad of aspartic acid, histidine and serine to catalyze the formation of a covalent intermediate with the substrate. There is a hydrophobic binding pocket to help align the protein with the enzyme, and an oxyanion hole to stabilize the intermediate. | + | Trypsin is a serine protease. It works with a catalytic triad of <scene name='Ann_Taylor_sandbox_120/Catalytic_triad/1'>aspartic acid, histidine and serine</scene> to catalyze the formation of a covalent intermediate with the substrate. There is a hydrophobic binding pocket to help align the protein with the enzyme, and an oxyanion hole to stabilize the intermediate. |
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| - | Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load | ||
| - | and display another structure. | ||
{{STRUCTURE_1taw | PDB=1taw | SCENE= }} | {{STRUCTURE_1taw | PDB=1taw | SCENE= }} | ||
Current revision
Trypsin bound to an inhibitor
Trypsin is a serine protease. It works with a catalytic triad of to catalyze the formation of a covalent intermediate with the substrate. There is a hydrophobic binding pocket to help align the protein with the enzyme, and an oxyanion hole to stabilize the intermediate.
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| 1taw, resolution 1.80Å () | |||||||||
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| Ligands: | |||||||||
| Gene: | A4 (Homo sapiens) | ||||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
