2DG5
Crystal Structure of Gamma-glutamyl transpeptidase from Escherichia coli in complex with hydrolyzed Glutathione
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, C (A, C) | Gamma-glutamyltranspeptidase | polymer | 366 | 39827.1 | 2 | UniProt (P18956) Pfam (PF01019) | Escherichia coli K12 | |
| 2 | B, D (B, D) | Gamma-glutamyltranspeptidase | polymer | 190 | 20263.0 | 2 | UniProt (P18956) Pfam (PF01019) | Escherichia coli K12 | |
| 3 | E (A) | GLYCEROL | non-polymer | 92.1 | 1 | Chemie (GOL) | |||
| 4 | F, H (B, D) | CALCIUM ION | non-polymer | 40.1 | 2 | Chemie (CA) | |||
| 5 | G, I (B, D) | GLUTAMIC ACID | non-polymer | 147.1 | 2 | Chemie (GLU) | |||
| 6 | J, K, L, M (A, B, C, D) | water | water | 18.0 | 867 | Chemie (HOH) |
Sequence modifications
A, C: 25 - 390 (UniProt: P18956)
B, D: 391 - 580 (UniProt: P18956)
| PDB | External Database | Details |
|---|---|---|
| Mse 50 | Met 50 | modified residue |
| Mse 99 | Met 99 | modified residue |
| Mse 116 | Met 116 | modified residue |
| Mse 125 | Met 125 | modified residue |
| Mse 164 | Met 164 | modified residue |
| Mse 233 | Met 233 | modified residue |
| Mse 255 | Met 255 | modified residue |
| Mse 290 | Met 290 | modified residue |
| Mse 312 | Met 312 | modified residue |
| Mse 323 | Met 323 | modified residue |
| Mse 326 | Met 326 | modified residue |
| PDB | External Database | Details |
|---|---|---|
| Mse 431 | Met 431 | modified residue |
| Mse 464 | Met 464 | modified residue |
| Mse 494 | Met 494 | modified residue |
| Mse 550 | Met 550 | modified residue |
| Mse 557 | Met 557 | modified residue |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 120180.0 | |
| Non-Polymers* | Number of molecules | 5 |
| Total formula weight | 466.5 | |
| All* | Total formula weight | 120646.6 |
