5XH3
Crystal structure of a novel PET hydrolase R103G/S131A mutant in complex with HEMT from Ideonella sakaiensis 201-F6
Summary for 5XH3
| Entry DOI | 10.2210/pdb5xh3/pdb |
| Related | 5XH2 |
| Descriptor | Poly(ethylene terephthalate) hydrolase, O 4-(2-hydroxyethyl) O 1-methyl benzene-1,4-dicarboxylate, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | poly(ethylene terephthalate) hydrolase, substrate binding, inhibitor, hydrolase |
| Biological source | Ideonella sakaiensis (strain 201-F6) |
| Cellular location | Secreted : A0A0K8P6T7 |
| Total number of polymer chains | 1 |
| Total formula weight | 27743.64 |
| Authors | Han, X.,Liu, W.D.,Zheng, Y.Y.,Chen, C.C.,Guo, R.T. (deposition date: 2017-04-19, release date: 2017-12-20, Last modification date: 2024-11-20) |
| Primary citation | Han, X.,Liu, W.,Huang, J.W.,Ma, J.,Zheng, Y.,Ko, T.P.,Xu, L.,Cheng, Y.S.,Chen, C.C.,Guo, R.T. Structural insight into catalytic mechanism of PET hydrolase Nat Commun, 8:2106-2106, 2017 Cited by PubMed Abstract: PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, and activity measurements, a substrate-binding mode is proposed, and several features critical for catalysis are elucidated. PubMed: 29235460DOI: 10.1038/s41467-017-02255-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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