Difference between revisions of "Part:BBa K3468025"
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<partinfo>BBa_K3468025 short</partinfo> | <partinfo>BBa_K3468025 short</partinfo> | ||
| − | + | The PETase is an enzyme, which can hydrolyze PET and this mutation protein is changed on the basis of the PETase.This mutant is more stable in higher temperature compared with the wild type. | |
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===Usage and Biology=== | ===Usage and Biology=== | ||
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| − | [[File:PETase A40P,S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,N275P.jpeg|400px | + | |
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| + | [[File:PETase A40P,S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,N275P.jpeg|400px]] | ||
| + | The benzene ring is located in a gully between two aromatic residues TYR87 and TRP185. | ||
| + | The distance of PI-PI bond is 5.0A between TRP185 and the benzene ring in part of the first MHET. | ||
| + | The whole ligand just fits into the pocket and binds tightly. | ||
| + | Three residues of Ser160, Asp206 and His237 formed a catalytic triplet, and ranging was performed: Y87:4.8A ;M161:5.4A; H237:4.9A. | ||
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| + | Significance of molecular docking for mutant work: | ||
| + | The molecular docking model can predict the binding mode and affinity of mutants and ligands, and promote the work of mutants by analyzing the result model. | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K3468025 parameters</partinfo> | <partinfo>BBa_K3468025 parameters</partinfo> | ||
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Revision as of 16:35, 27 October 2020
PETase S54W,T113P,T116R,Q119D,Q127L,Q182I,S193R,S214F,K252L,R260F,T266P,N275P The PETase is an enzyme, which can hydrolyze PET and this mutation protein is changed on the basis of the PETase.This mutant is more stable in higher temperature compared with the wild type. Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 240
- 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 240
- 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 240
- 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 240
- 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 240
- 1000COMPATIBLE WITH RFC[1000]
The benzene ring is located in a gully between two aromatic residues TYR87 and TRP185.
The distance of PI-PI bond is 5.0A between TRP185 and the benzene ring in part of the first MHET.
The whole ligand just fits into the pocket and binds tightly.
Three residues of Ser160, Asp206 and His237 formed a catalytic triplet, and ranging was performed: Y87:4.8A ;M161:5.4A; H237:4.9A.
Significance of molecular docking for mutant work: The molecular docking model can predict the binding mode and affinity of mutants and ligands, and promote the work of mutants by analyzing the result model.