Pub. Date : 2013
PMID : 23633953
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI. | ospi | ubiquitin conjugating enzyme E2 N | Homo sapiens |
| 2 | A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI. | ospi | ubiquitin conjugating enzyme E2 N | Homo sapiens |
| 3 | A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI. | ospi | ubiquitin conjugating enzyme E2 N | Homo sapiens |
| 4 | A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI. | ospi | ubiquitin conjugating enzyme E2 N | Homo sapiens |
| 5 | The OspI-binding sites in Ubc13 largely overlap with the binding residues for host ubiquitin E3 ligases and a deubiquitinating enzyme, which suggests that the bacterial effector and host proteins exploit the same surface on Ubc13 for specific recognition. | ospi | ubiquitin conjugating enzyme E2 N | Homo sapiens |
| 6 | The OspI-binding sites in Ubc13 largely overlap with the binding residues for host ubiquitin E3 ligases and a deubiquitinating enzyme, which suggests that the bacterial effector and host proteins exploit the same surface on Ubc13 for specific recognition. | ospi | ubiquitin conjugating enzyme E2 N | Homo sapiens |