GST_N: Glutathione S-transferase, N-terminal domain
| PAG Title | GST_N: Glutathione S-transferase, N-terminal domain |
| PAG ID | PEX001140 |
| Type | A |
| Source Link |  Pfam |
| Publication Reference | NA |
| PAG Description | Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognised); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognised). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain 1. |
| Species | Homo sapiens |
| Quality Metric Scores | nCoCo Score: 0 |
| Information Content | Poor |
| Other IDs | PF02798 |
| Base PAG ID | PEX001140 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
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