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- Image:ICCG sub.pdb (0 bytes)
- Image:ICCG sep.pdb (0 bytes)
- Image:ICCG.pdb (0 bytes)
- Image:ICCG substrate.pdb (0 bytes)
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- 9qyt (2,483 bytes)
2: ...structure of leaf branch compost cutinase variant ICCG L50Y T110E==
7: ...and=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qyt ProSAT]</span></td></tr> - 9qyu (2,516 bytes)
2: ...of leaf branch compost cutinase quintuple variant ICCG L50Y==
7: ...bligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qyu ProSAT]</span></td></tr> - 9qyq (2,427 bytes)
2: ...structure of leaf branch compost cutinase variant ICCG L50Y T26E==
7: ...<td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qyq ProSAT]</span></td></tr> - 9qyr (2,429 bytes)
2: ...structure of leaf branch compost cutinase variant ICCG L50Y Q183K==
7: ...<td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qyr ProSAT]</span></td></tr> - 9qys (2,478 bytes)
2: ...structure of leaf branch compost cutinase variant ICCG L50Y Q238K==
7: ...bligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qys ProSAT]</span></td></tr> - User:David Bogle/Sandbox 2 (3,116 bytes)
4: <scene name='10/1076054/Iccg_disulfide_bridge/4'>Disulfide Bridge white</scene...
6: <scene name='10/1076054/Iccg_disulfide_bridge/6'>Disulfide Bridge blue</scene>
28: ... the substrate 2-HE(MHET)3 in wild-type LLC (4eb0.pdb) was constructed and refined to mimic the 3D stru...
43: ====PDB Files====
44: PDB Files - Justin Chavez/Sandbox1 (935 bytes)
1: =''ICCG, Pet Hydroalse''=
2: ...CG Pet Hydrolase - 6THT' scene='10/1075218/Mutant_pdb/3'> - 8ota (4,146 bytes)
7: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ota ProSAT]</span></td></tr>
13: ...ere, we explore this aspect in the context of LCC(ICCG), an optimized PETase, derived from the leaf-bran...
19: <div class="pdbe-citations 8ota" style="background-color:#fffaf0;... - 8jmo (4,533 bytes)
2: ==Structure of a leaf-branch compost cutinase, ICCG in complex with 4-((4-Hydroxybutoxy)carbonyl)benz...
7: ...dbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=E7J:4-(4-oxidanylbutoxycarbonyl)benzoic+aci...
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jmo ProSAT]</span></td></tr>
20: <div class="pdbe-citations 8jmo" style="background-color:#fffaf0;... - 8jmp (4,539 bytes)
2: ==Structure of a leaf-branch compost cutinase, ICCG in complex with 1,4-butanediol terephthalate==
7: ...dbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EMX:4-[4-(4-carboxyphenyl)carbonyloxybutoxy...
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jmp ProSAT]</span></td></tr>
20: <div class="pdbe-citations 8jmp" style="background-color:#fffaf0;... - 8qrj (4,756 bytes)
2: ==LCC-ICCG PETase mutant H218Y==
7: ...and=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL...
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qrj ProSAT]</span></td></tr>
14: ...rovement. Analysis of the solved structure of LCC-ICCG/H218Y compared to other known PETases featuring d...
20: <div class="pdbe-citations 8qrj" style="background-color:#fffaf0;... - 9kl9 (3,366 bytes)
7: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9kl9 ProSAT]</span></td></tr>
13: ... superior to benchmarks Kubu-P(M12) (83%) and LCC-ICCG (71%). Overall, the engineered PET hydrolases dem...
19: <div class="pdbe-citations 9kl9" style="background-color:#fffaf0;... - User:Mark Macbeth/SandboxJustin (900 bytes)
1: =''ICCG PET Hydrolase''=
3: ...ize='350' frame='true' side='right' caption='ICCG PDB:6tht' scene=''> - User:Hayden Vissing/Sandbox 1 (13,923 bytes)
2: ...HT' size='350' frame='true' side='right' caption='ICCG PET Hydrolase - 6THT' scene='10/1076051/Mutant_ov...
13: ...>LCC</scene><ref name="main">PMID:32269349</ref> (PDB: 4EB0<ref name="4eb0">Sulaiman S, You DJ, Eiko K,...
23: ... the substrate 2-HE(MHET)3 in wild-type LLC (4eb0.pdb) was constructed and refined to mimic the 3D stru...
30: ...051/Mutant_overview_shade/3'>ICCG</scene> enzyme (PDB: 6THT<ref name="6tht">Sulaiman S, You DJ, Eiko K,...
34: ...rrows labeled A on the LCC wild type and B on the ICCG mutant. These arrows point to the loss of the “... - User:Mark Macbeth/Sandbox13 (13,468 bytes)
60: ...e name='10/1075193/F243i/4'>F243I</scene> (in the ICCG mutant) and <scene name='10/1075193/F243w_mutant/...
71: ...d 53% depolymerization in 20 hours while both the ICCG and WCCG mutants reached 90% depolymerization in ...
73: The ICCG and WCCG mutations constructed by Tournier et al.... - User:Anjali Rabindran/Sandbox 1 (6,231 bytes)
1: ... caption='Leaf-branch compost bacterial cutinase, PDBID: 4EB0' scene='10/1075191/Wild_type_pet_hydrolas...
25: ...ubstrate</scene> (2-HE(MHET)₃) onto the enzyme (PDB ID 4EB0). The site, mainly a hydrophobic pocket, ...
35: ...pecific activity and rate of wild-type, WCCG, and ICCG mutants. Initial rate was measured by the calcula...
51: | ICCG
56: ...uggests that the mutations introduced in WCCG and ICCG enhance the rate of PET breakdown.</p> - Engineering of Leaf-branch Compost Bacterial Cutinase for PET Degradation (24,346 bytes)
1: ... caption='Leaf-branch compost bacterial cutinase, PDBID: 4EB0' scene='10/1075191/Wild_type_pet_hydrolas...
20: ...ondary structure of Leaf-branch compost cutinase (PDB ID: 4EB0). Diagram from [https://www.ebi.ac.uk/ E...
64: ...el of the substrate 2-HE(MHET)3 in wild-type LLC (PDB ID: 4EB0) was constructed and refined to mimic th...
106: ...pecific activity and rate of wild-type, WCCG, and ICCG mutants. </b>Initial rate was measured by the cal...
122: | ICCG - User:Emily Hwang/Sandbox1 (21,051 bytes)
1: ... caption='Leaf-branch compost bacterial cutinase, PDBID: 4EB0' scene='10/1075193/Wild_type_pet_hydrolas...
60: ...ubstrate</scene> (2-HE(MHET)₃) onto the enzyme (PDB ID 4EB0). The site, mainly a hydrophobic pocket, ...
66: ...pecific activity and rate of wild-type, WCCG, and ICCG mutants. Initial rate was measured by the calcula...
85: <th style="width:0%"><td>ICCG</td>
91: ...uggests that the mutations introduced in WCCG and ICCG enhance the rate of PET breakdown. - 7w66 (3,867 bytes)
7: ...<td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8X:bis(2-hydroxyethyl)+benzene-1,4-dicarbo...
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w66 ProSAT]</span></td></tr>
12: ... PET materials 2.2-fold more efficiently than LCC ICCG, which was previously the most active PET hydrola...
18: <div class="pdbe-citations 7w66" style="background-color:#fffaf0;... - 7w69 (3,833 bytes)
7: ...<td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
8: ...Bsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w69 ProSAT]</span></td></tr>
12: ... PET materials 2.2-fold more efficiently than LCC ICCG, which was previously the most active PET hydrola...
18: <div class="pdbe-citations 7w69" style="background-color:#fffaf0;...
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