1GAE
COMPARISON OF THE STRUCTURES OF WILD TYPE AND A N313T MUTANT OF ESCHERICHIA COLI GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASES: IMPLICATION FOR NAD BINDING AND COOPERATIVITY
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | O, P | D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE | polymer | 330 | 35433.2 | 2 | UniProt (P0A9B2) Pfam (PF00044) Pfam (PF02800) In PDB | Escherichia coli | |
| 2 | O, P | NICOTINAMIDE-ADENINE-DINUCLEOTIDE | non-polymer | 663.4 | 2 | Chemie (NAD) | |||
| 3 | water | water | 18.0 | 279 | Chemie (HOH) |
Sequence modifications
O, P: 0 - 330 (UniProt: P0A9B2)
| PDB | External Database | Details |
|---|---|---|
| Thr 313 | Asn 313 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 70866.5 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 1326.8 | |
| All* | Total formula weight | 72193.3 |
