6LGK
Crystal structure of an oxido-reductase with mutation
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B, C, D (A, B, C, D) | Glyceraldehyde-3-phosphate dehydrogenase | polymer | 333 | 35835.9 | 4 | UniProt (P16858) Pfam (PF00044) Pfam (PF02800) | Mus musculus (Mouse) | GAPDH,Peptidyl-cysteine S-nitrosylase GAPDH,oxido-reductase |
| 2 | E, H, K (A, B, C) | NICOTINAMIDE-ADENINE-DINUCLEOTIDE | non-polymer | 663.4 | 3 | Chemie (NAD) | |||
| 3 | F, G, I, J, L... (A, B, C) | PHOSPHATE ION | non-polymer | 95.0 | 6 | Chemie (PO4) | |||
| 4 | N, O, P, Q (A, B, C, D) | water | water | 18.0 | 1157 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 3 - 335 (UniProt: P16858)
| PDB | External Database | Details |
|---|---|---|
| Ser 152 | Cys 150 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 143343.6 | |
| Non-Polymers* | Number of molecules | 9 |
| Total formula weight | 2560.1 | |
| All* | Total formula weight | 145903.7 |
