GST_C: Glutathione S-transferase, C-terminal domain
| PAG Title | GST_C: Glutathione S-transferase, C-terminal domain |
| PAG ID | PEX002045 |
| Type | A |
| Source Link |  Pfam |
| Publication Reference | NA |
| PAG Description | GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain 1. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes 2. |
| Species | Homo sapiens |
| nCoCo Score | 0 |
| Base PAG ID | PEX002045 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
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