1LBK
Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B | Glutathione S-transferase class pi chimaera (CODA) | polymer | 208 | 23238.6 | 2 | UniProt (P09211) UniProt (P08263) Pfam (PF02798) Pfam (PF14497) In PDB | Homo sapiens (human) | |
2 | A, B | 2-(N-MORPHOLINO)-ETHANESULFONIC ACID | non-polymer | 195.2 | 2 | Chemie (MES) | |||
3 | A, B | GLUTATHIONE | non-polymer | 307.3 | 2 | Chemie (GSH) | |||
4 | B | SULFATE ION | non-polymer | 96.1 | 1 | Chemie (SO4) | |||
5 | water | water | 18.0 | 450 | Chemie (HOH) |
Sequence modifications
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 46477.2 | |
Non-Polymers* | Number of molecules | 5 |
Total formula weight | 1101.2 | |
All* | Total formula weight | 47578.4 |