2DBU
Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli
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, F, G, H (A, B, C, D) | water | water | 18.0 | 605 | 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 | |
All* | Total formula weight | 120180.0 |